PML (gen)

PML (gen)
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1BOR, 2MVW, 2MWX, 4WJN, 4WJO
Identifikatori
Aliasi	PML
Vanjski ID-jevi	OMIM: 102578 MGI: 104662 HomoloGene: 13245 GeneCards: PML
Lokacija gena (čovjek)
Hrom.	Hromosom 15 (čovjek)
Kraj	74,047,827 bp
Lokacija gena (miš)
Hrom.	Hromosom 9 (miš)
Kraj	58,157,069 bp
Ontologija gena
Molekularna funkcija	• SUMO binding; • cobalt ion binding; • vezivanje iona metala; • protein homodimerization activity; • vezivanje iona cinka; • GO:0001948, GO:0016582 vezivanje za proteine; • SMAD binding; • vezivanje sa DNK; • GO:0001105 transcription coactivator activity; • protein heterodimerization activity; • ubiquitin protein ligase binding; • SUMO transferase activity;
Ćelijska komponenta	• citoplazma; • citosol; • endozom; • Jedarna membrana; • membrana; • jedro; • nuclear matrix; • Jedarce; • Endoplazmatski retikulum; • early endosome membrane; • intracellular anatomical structure; • nukleoplazma; • PML body; • endoplasmic reticulum membrane; • extrinsic component of endoplasmic reticulum membrane; • GO:0035328 heterochromatin;
Biološki proces	• regulation of protein phosphorylation; • positive regulation of histone deacetylation; • intrinsic apoptotic signaling pathway in response to oxidative stress; • myeloid cell differentiation; • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; • negative regulation of telomere maintenance via telomerase; • rhythmic process; • interferon-gamma-mediated signaling pathway; • negative regulation of telomerase activity; • positive regulation of telomere maintenance; • Ćelijsko starenje; • regulation of cell adhesion; • defense response to virus; • intrinsic apoptotic signaling pathway in response to DNA damage; • positive regulation of extrinsic apoptotic signaling pathway; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • transforming growth factor beta receptor signaling pathway; • proteasome-mediated ubiquitin-dependent protein catabolic process; • negative regulation of cell population proliferation; • positive regulation of defense response to virus by host; • GO:0097285 apoptoza; • response to cytokine; • cell fate commitment; • negative regulation of translation in response to oxidative stress; • GO:0009373 regulation of transcription, DNA-templated; • common-partner SMAD protein phosphorylation; • branching involved in mammary gland duct morphogenesis; • extrinsic apoptotic signaling pathway; • positive regulation of fibroblast proliferation; • positive regulation of apoptotic signaling pathway; • endoplasmic reticulum calcium ion homeostasis; • transcription, DNA-templated; • PML body organization; • negative regulation of cell growth; • intrinsic apoptotic signaling pathway by p53 class mediator; • Urođeni imunski sistem; • GO:0022415 viral process; • response to gamma radiation; • response to UV; • regulation of calcium ion transport into cytosol; • positive regulation of protein localization to chromosome, telomeric region; • fibroblast migration; • Ciljanje proteina; • immune system process; • protein stabilization; • positive regulation of apoptotic process involved in mammary gland involution; • circadian regulation of gene expression; • regulation of MHC class I biosynthetic process; • regulation of circadian rhythm; • GO:0045996 negative regulation of transcription, DNA-templated; • maintenance of protein location in nucleus; • cellular response to interleukin-4; • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; • response to hypoxia; • regulation of double-strand break repair; • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; • retinoic acid receptor signaling pathway; • negative regulation of angiogenesis; • negative regulation of ubiquitin-dependent protein catabolic process; • entrainment of circadian clock by photoperiod; • negative regulation of mitotic cell cycle; • positive regulation of MHC class I biosynthetic process; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • regulation of signal transduction by p53 class mediator; • cellular response to leukemia inhibitory factor; • protein import into nucleus; • GO:0034622 protein-containing complex assembly; • positive regulation of nucleic acid-templated transcription; • protein sumoylation;
	Izvori:Amigo / QuickGO
Ortolozi
	5371
	18854
	ENSG00000140464
	ENSMUSG00000036986
	P29590
	Q60953
NM_033250; NM_002675; NM_033238; NM_033239; NM_033240;
	NM_033244; NM_033246; NM_033247; NM_033249
	NM_008884; NM_178087; NM_001311088
NP_002666; NP_150241; NP_150242; NP_150243; NP_150247;
	NP_150249; NP_150250; NP_150252; NP_150253
	NP_001298017; NP_032910; NP_835188
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Protein promijelocitne leukemije (PML), znan i kao MYL, RNF71, PP8675 ili TRIM19^[5]) je proteinski proizvod kodiran genom PML. PML je proteinski supresor tumora, potreban za sastavljanje niza jedarnih struktura, nazvanih PML-jedarna tijela, koja se formiraju u hromatinu^[5] ćelijskog jedra. Ova jedarna tijela prisutna su u jedrima sisara, otprilike 1 – 30 po jezdru.^[5] Poznato je da PML-NB imaju brojne regulatorne ćelijske funkcije, uključujući uključenost u programiranu ćelijsku smrt, stabilnost genoma, antivirusne efekte i kontrolu ćelijske diobe.^[5]^[6] Mutacija ili gubitak PML-a i posljedična disregulacija ovih procesa uključeni su u razne karcinome.<name="Bernardi_2007"/> 2017}}</ref>

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 882 aminokiseline, a molekulska težina 97.551 Da ^[7].

10	20	30	40	50
MEPAPARSPR	PQQDPARPQE	PTMPPPETPS	EGRQPSPSPS	PTERAPASEE
EFQFLRCQQC	QAEAKCPKLL	PCLHTLCSGC	LEASGMQCPI	CQAPWPLGAD
TPALDNVFFE	SLQRRLSVYR	QIVDAQAVCT	RCKESADFWC	FECEQLLCAK
CFEAHQWFLK	HEARPLAELR	NQSVREFLDG	TRKTNNIFCS	NPNHRTPTLT
SIYCRGCSKP	LCCSCALLDS	SHSELKCDIS	AEIQQRQEEL	DAMTQALQEQ
DSAFGAVHAQ	MHAAVGQLGR	ARAETEELIR	ERVRQVVAHV	RAQERELLEA
VDARYQRDYE	EMASRLGRLD	AVLQRIRTGS	ALVQRMKCYA	SDQEVLDMHG
FLRQALCRLR	QEEPQSLQAA	VRTDGFDEFK	VRLQDLSSCI	TQGKDAAVSK
KASPEAASTP	RDPIDVDLPE	EAERVKAQVQ	ALGLAEAQPM	AVVQSVPGAH
PVPVYAFSIK	GPSYGEDVSN	TTTAQKRKCS	QTQCPRKVIK	MESEEGKEAR
LARSSPEQPR	PSTSKAVSPP	HLDGPPSPRS	PVIGSEVFLP	NSNHVASGAG
EAEERVVVIS	SSEDSDAENS	SSRELDDSSS	ESSDLQLEGP	STLRVLDENL
ADPQAEDRPL	VFFDLKIDNE	TQKISQLAAV	NRESKFRVVI	QPEAFFSIYS
KAVSLEVGLQ	HFLSFLSSMR	RPILACYKLW	GPGLPNFFRA	LEDINRLWEF
QEAISGFLAA	LPLIRERVPG	ASSFKLKNLA	QTYLARNMSE	RSAMAAVLAM
RDLCRLLEVS	PGPQLAQHVY	PFSSLQCFAS	LQPLVQAAVL	PRAEARLLAL
HNVSFMELLS	AHRRDRQGGL	KKYSRYLSLQ	TTTLPPAQPA	FNLQALGTYF
EGLLEGPALA	RAEGVSTPLA	GRGLAERASQ	QS

Simboli

C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin

Struktura

Gen PML dugačak je otprilike 53 kilobaznih parova i nalazi se na q kraku hromosoma 15. Sastoji se od 10 egzona koji su podložni mijenjanju putem alternativne prerade, što daje više od 15 poznatih PML proteinskih izoformi.^[8]^[9] Iako se izoforme razlikuju na svom C-terminalnom domenu, sve sadrže TRIpartitni motiv kodiran sa prva tri genska egzona.^[10] TRIpartitni motiv sastoji se od cinka cinkovog prstena, dva sredstva za vezivanje cinkivog domena, zvanog B1 i B2 kutija, i RBCC dimerizacijskog domena, sastavljenog od dva alfa-heliksna domena zavojnice.^[9]

Gen PML je pod kontrolom u transkripcijskoj, translacijskoj i posttranslacijskoj kontroli. Područje promotora gena sadrži ciljeve pretvarača signala i aktivatora transkripcije (STAT), refulacijski faktor interferona i protein p53, što ukazuje na zamršenost njegovog učešća u ćelijskim funkcijama.^[11] Pored regulacije putem alternativne prerade, proteinski proizvod podliježe posttranslacijskim modifikacijama, kao što su acetilacija i fosforilacija. C-kraj sadrži ostatke serina koje fosforilizira kazein-kinazama, a postoji i nekoliko ostataka tirozina i treonina koji također mogu biti ciljevi fosforilacije.^[9] PML fosforilacija pokreće daljnju modifikaciju vezivanjem proteina SUMO na RING domen pomoću UBC9 SUMO-konjugirajućeg enzima,^[5] koji je ovisan o ćelijskom ciklusu. PML sadrži domen koja veže SUMO koji jeneophodan za njegovu interakciju s drugim SUMOiliziranim proteinima, kao što su on sam i mnogi drugi.^[9] I ubikvitinacija i SUMOilacija PML proteina mogu podstaknuti njegovu degradaciju u proteasom, pružajući na taj način sredstvo za moduliranje labilnosti PML proteina unutar ćelije.^[11]

PML se prenosi u citoplazmu ćelije, ali njegov N-kraj sadrži signal lokalizacije jedarne energije, što uzrokuje njegov unos u jesdro. U jedru, sumoilirani PML proteini se međusobno multimeriziraju interakcijama na RBCC domenu. Ovo stvara prstenastu strukturu koja se veže za jedarnu matricu, formirajući PML-jedarno tijelo (PML-NB). Na rubu prstenastog proteinskog multimera nalaze se proteinske niti koje se protežu iz prstena i uspostavljaju kontakt s hromatinskim vlaknima.^[5] Ovo održava položaj PML-NB unutar jedra, kao i stabilnost proteina. Kada je hromatin pod stresom, naprimjer za vrijeme apoptoza, PML-NB postaje nestabilan i PML-a tijela se preraspodjeljuju u mikrostrukture. Ove mikrostrukture sadrže PML protein, ali ne i mnogo interaktivnih proteina koji su obično povezani sa PML-NB.^[5]^[12]

PML-NB nisu nasumično raspoređeni po jedru, već se nalaze unutar njega i obično su povezani sa drugim jedarnim tijelima kao što su spojne tačke i jedarca, kao i regijama koje su bogate genima i aktivno se transkribiraju. Naročito je pokazano da se PML-NB povezuju s genima kao što je MHC I klaster gena, kao i gen p53. Tačan značaj ove povezanosti nije jasan, ali dokazi sugeriraju da PML-NB mogu uticati na transkripciju na ovim specifičnim genskim mjestima.^[13]

Funkcija

PML-NB imaju širok spektar funkcija i veliku ulogu u regulaciji ćelija. Svoj široki spektar djelovanja ostvaruju interakcijama sa različitim proteinima lokalizovanim u PML-NB. Smatra se da specifična biohemijska funkcija koju izvode PML-NB može služiti kao E3 ligaza za sumoilaciju drugih proteina.^[5] Istinska funkcija, međutim, ostaje nejasna i predloženo je nekoliko mogućih modela za funkciju PML-NB, uključujući jedarno skladištenje proteina, koje služe kao pristanište na kojem se akumuliraju drugi proteini da bi bili posttranslacijski modificirani, uz direktno sudjelovanje u transkripciji i regulaciji hromatina.^[14]

PML-NB takođe imaju ulogu u regulaciji transkripcije. Pokazalo se da PML-NB pojačavaju transkripciju nekih gena, istovremeno potiskujući transkripciju drugih.^[5] Predloženo je da mehanizam pomoću kojeg PML-NB to rade putem procese preuređivanja hromatina, iako je to neizvjesno.^[5]

Zbog ove očite kontradikcije, moguće je da PML-NB mogu biti heterogene strukture, koje imaju različite funkcije na osnovu smještaja unutar jedra, proteina s kojima stupaju u interakciju u određenom području jedra ili specifičnih izoformi PML proteina od kojih su sastavljeni.

Pored ove regulacije transkripcije, zapažanja o PML-NBs snažno sugeriraju da kompleks proteina ima ulogu u posredovanju odgovora na oštećenje DNK. Naprimjer, broj i veličina PML-NB povećavaju se kako se povećavaju aktivnosti senzora oštećenja DNK ATM i Ataxia telangiectasia i Rad3-stodni ATR. Jedarna tijela se lokaliziraju na mjestu oštećenja DNK, gdje se proteini povezani sa popravcima DNK i zaustavljanjem ćelijskog ciklusa zatim lokaliziraju.^[13] Funkcionalna svrha interakcije između PML-NB i mehanizama za obnavljanje DNK ostaje nejasna, ali čini se malo vjerojatnim da oni imaju ulogu u izravnom popravljanju DNK, zbog kolokalizacije proteina za popravak DNK i PML-NB neko vrijeme nakon što je DNK oštećena. Umjesto toga, smatra se da PML-NB mogu regulirati reakcije na oštećenja DNK djelujući kao mjesto skladištenja proteina koji sudjeluju u popravljanju DNK, regulirajući izravno popravak ili posredujući između popravljanja DNK i odgovora na kontrolnim tačkama.^[5] Međutim, jasno je da PML-NB imaju ulogu u posredovanju odgovora na kontrolnim tačkama, posebno u izazivanju apoptoza.

PML ima važnu ulogu u p53 ovisnom i o p53 neovisnom apoptotskom putu. PML aktivira p53 regrutovanjem proteina na mjesto PML-NBs i promoviranjem njegove aktivacije, dok istovremeno inhibira regulatore proteina kao što su MDM2 ili Herpes virus povezan sa ubikvitin-specifičnom proteazom (HAUSP).^[5] Na putevima koji ne koriste p53 u indukciji apoptoze, pokazalo se da PML stupa u interakciju sa CHK2 i indukuje ga da autofosforilira kako bi postao aktivan.^[5] Pored toga na ta dva apoptotska puta, Fas-indukovana apoptoza oslanja se na PML-NB da oslobode FLICE-pridruženi ogromni protein, koji se zatim lokalizuje u mitohondrije da pospješi aktivaciju kaspaze-8.^[5]

Osim apoptoze, druge studije uključuju PML-NB u ćelijsku senescenciju, posebno njenu indukciju.^[5] Pokazalo se da je uključeno u stvaranje nekih hromatinskih karakteristika ćelija koje imaju starenje, poput žarišta heterohromatina povezanih sa senescencijom (SAHF), za koje se vjeruje da potiskuju ekspresiju faktora i gena koji potiču rast. Stvaranje ovih karakteristika rezultat je histonskih šaperona, HIRA i ASF1, čije prepravljanje hromatina ovdje posreduju PML-NB. HIRA se lokalizira na PML-NB prije nego što se dogodi bilo kakva druga interakcija s DNK.^[5]

Uloga u kanceru

Gubitak funkcionalne mutacije proteina PML, posebno rezultat fuzije gena PML sa genom RARα u akutnoj promelocitnoj leukemiji, impliciran je u nekoliko tumora koji suzbijaju apoptotske puteve, posebno one koji se oslanjaju na p53, kao što je gore navedeno.^[5]^[14] Dakle, gubitak funkcije PML daje prednost ćelijskom preživljavanju i proliferaciji, sprečava ćelijski starenje gubitkom SAHF-a i stavlja blokadu ćelijskoj diferencijaciji.^[14]

Utvrđeno je da, nakon gubitka funkcije PML, i ljudi i miševi pokazuju povećanu sklonost stvaranju tumora. Prekid PML-a javlja se u širokom spektru tipova karcinoma, što rezultira više metastatskim tumorima i shodno tome lošim prognozama.^[14] Smatra se da, osim važnosti koju ima u apoptotskim ulogama, inaktivacija PML-a može prouzrokovati da u ćelijama favorizuju napredovanje tumora, omogućavajući da akumuliraju dodatna genetička oštećenja. Mnogi proteini koji su uključeni u održavanje genomske stabilnosti oslanjaju se na PML-NB za ciljanje, a gubitak PML-a dovodi do smanjenja efikasnosti popravka unutar ćelije.^[14]

Uloga u ćelijskom ciklusu

Raspodela i koncentracija PML-NB se menjaju dok se ćelija prolazi kroz ćelijski ciklus. U G0 fazi prisutno je malo sumoiliranih PML-NB, ali njihov se broj povećava kako ćelija napreduje kroz faze, od G1 do S do G2. Tokom kondenzacije hromatina koja se javlja tokom mitoza, desumoilacija PML-a uzrokuje disocijaciju mnogih povezanih faktora, a PML proteini se samo agregiraju i formiraju nekoliko velikih agregata nazvanih mitotskim nakupinama PML proteina (MAPP).^[5] Pored promjene broja, PML-NB se također povezuju s različitim proteinima toom životnog ciklusa i podvrgavaju se značajnim biohemijskim promjenama u sastavu.^[5]

Tokom S faze ćelijskog ciklusa, kompleksi PML-NB se raspadaju, dok se njihova hromatinska skela mijenja tokom replikacije. Fizičko razbijanje PML-NB na manje fragmente promovira stvaranje više PML-NB koji postoje u G2, ali nivo ekspresije proteina PML nije povećan.^[5] Smatra se da da ovo može poslužiti za očuvanje orijentacije hromatida s kojima su povezani PML-NB ili za praćenje integriteta replikacijske viljuške.^[5]

Antivirusne funkcije

Transkripcija PML-a povećana je prisustvom interferona α/β i γ. Smatra se da povećani broj PML-NB koji su rezultat ovog povećanja ekspresije PML proteina može rezultirati sekvestriranjem virusnih proteina u PML-NB. Dakle, virus ih nije u stanju iskoristiti. Proteini koje drže PML-NB su tada sumoilirani, trajno deaktivirajući virione.^[6]

Interakcije

Pokazalo se da protein promelocitne leukemije ima interakcije sa:

ANKRD2,^[15]
CREB-vezujući protein,^[16]^[17]^[18]
Ciklin T1,^[19]
Protein 6 pridružen smrti,^[20]^[21]^[22]^[23]
GATA2,^[24]
HDAC1,^[25]^[26]
HDAC3,^[26]
HHEX,^[27]
MAPK11,^[28]
MYB,^[29]
Mdm2,^[30]^[31]^[32]^[33]
Nerve Growth factor IB,^[34]
Jedarni receptor korepresora 1,^[25]
Jedarni receptor korepresora 2,^[25]^[35]
P53,^[30]^[36]^[37]
RPL11,^[31]
Retinoblastomski protein,^[38]
Retinoic acid receptor alpha,^[16]
SIN3A,^[25]
SKI protein,^[25]
STAT3,^[39]
Serum response factor^[17] and
Mali ubikvitinu-srodni modifikator 1,^[40]^[41]
Sp1 transcripcijski faktor,^[42]
TOPBP1,^[43]
Timin-DNK glikozulaza,^[44] i
Protein 16 cinkovog prsta sa BTB-domenom.^[45]

Također pogledajte

Domen RING prsta

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000140464 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036986 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k ^l ^m ⁿ ^o ^p ^q ^r ^s ^t ^u Bernardi R, Pandolfi PP (decembar 2007). "Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies". Nature Reviews. Molecular Cell Biology. 8 (12): 1006–16. doi:10.1038/nrm2277. PMID 17928811.
^ ^a ^b Sahin U, Lallemand-Breitenbach V, de Thé H (novembar 2014). "PML nuclear bodies: regulation, function and therapeutic perspectives". The Journal of Pathology (jezik: engleski). 234 (3): 289–91. doi:10.1002/path.4426. PMID 25138686.
^ "UniProt, P29590". Pristupljeno 16. 7. 2021.
^ "PML promyelocytic leukemia [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Pristupljeno 6. 12. 2016.
^ ^a ^b ^c ^d Pearson M, Pelicci PG (2001). "PML interaction with p53 and its role in apoptosis and replicative senescence". Oncogene. 20 (49): 7250–6. doi:10.1038/sj.onc.1204856. PMID 11704853.
^ Tang MK, Liang YJ, Chan JY, Wong SW, Chen E, Yao Y, Gan J, Xiao L, Leung HC, Kung HF, Wang H, Lee KK (21. 3. 2013). "Promyelocytic leukemia (PML) protein plays important roles in regulating cell adhesion, morphology, proliferation and migration". PLOS ONE. 8 (3): e59477. doi:10.1371/journal.pone.0059477. PMC 3605454. PMID 23555679.
^ ^a ^b Zhou W, Bao S (mart 2014). "PML-mediated signaling and its role in cancer stem cells". Oncogene (jezik: engleski). 33 (12): 1475–84. doi:10.1038/onc.2013.111. PMID 23563177.
^ Ching RW, Dellaire G, Eskiw CH, Bazett-Jones DP (mart 2005). "PML bodies: a meeting place for genomic loci?". Journal of Cell Science (jezik: engleski). 118 (Pt 5): 847–54. doi:10.1242/jcs.01700. PMID 15731002.
^ ^a ^b Dellaire G, Bazett-Jones DP (septembar 2004). "PML nuclear bodies: dynamic sensors of DNA damage and cellular stress". BioEssays (jezik: engleski). 26 (9): 963–77. doi:10.1002/bies.20089. PMID 15351967.
^ ^a ^b ^c ^d ^e Gurrieri C, Capodieci P, Bernardi R, Scaglioni PP, Nafa K, Rush LJ, Verbel DA, Cordon-Cardo C, Pandolfi PP (februar 2004). "Loss of the tumor suppressor PML in human cancers of multiple histologic origins". Journal of the National Cancer Institute (jezik: engleski). 96 (4): 269–79. doi:10.1093/jnci/djh043. PMID 14970276.
^ Kojic S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, Valle G, Faulkner G (maj 2004). "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle". Journal of Molecular Biology. 339 (2): 313–25. doi:10.1016/j.jmb.2004.03.071. PMID 15136035.
^ ^a ^b Zhong S, Delva L, Rachez C, Cenciarelli C, Gandini D, Zhang H, Kalantry S, Freedman LP, Pandolfi PP (novembar 1999). "A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins". Nature Genetics. 23 (3): 287–95. doi:10.1038/15463. PMID 10610177.
^ ^a ^b Matsuzaki K, Minami T, Tojo M, Honda Y, Saitoh N, Nagahiro S, Saya H, Nakao M (mart 2003). "PML-nuclear bodies are involved in cellular serum response". Genes to Cells. 8 (3): 275–86. doi:10.1046/j.1365-2443.2003.00632.x. PMID 12622724.
^ Doucas V, Tini M, Egan DA, Evans RM (mart 1999). "Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling". Proceedings of the National Academy of Sciences of the United States of America. 96 (6): 2627–32. doi:10.1073/pnas.96.6.2627. PMC 15819. PMID 10077561.
^ Marcello A, Ferrari A, Pellegrini V, Pegoraro G, Lusic M, Beltram F, Giacca M (maj 2003). "Recruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML protein". The EMBO Journal. 22 (9): 2156–66. doi:10.1093/emboj/cdg205. PMC 156077. PMID 12727882.
^ Ishov AM, Sotnikov AG, Negorev D, Vladimirova OV, Neff N, Kamitani T, Yeh ET, Strauss JF, Maul GG (oktobar 1999). "PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1". The Journal of Cell Biology. 147 (2): 221–34. doi:10.1083/jcb.147.2.221. PMC 2174231. PMID 10525530.
^ Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD (mart 2000). "Sequestration and inhibition of Daxx-mediated transcriptional repression by PML". Molecular and Cellular Biology. 20 (5): 1784–96. doi:10.1128/mcb.20.5.1784-1796.2000. PMC 85360. PMID 10669754.
^ Lehembre F, Müller S, Pandolfi PP, Dejean A (januar 2001). "Regulation of Pax3 transcriptional activity by SUMO-1-modified PML". Oncogene. 20 (1): 1–9. doi:10.1038/sj.onc.1204063. PMID 11244500.
^ Zhong S, Salomoni P, Ronchetti S, Guo A, Ruggero D, Pandolfi PP (februar 2000). "Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis". The Journal of Experimental Medicine. 191 (4): 631–40. doi:10.1084/jem.191.4.631. PMC 2195846. PMID 10684855.
^ Tsuzuki S, Towatari M, Saito H, Enver T (septembar 2000). "Potentiation of GATA-2 activity through interactions with the promyelocytic leukemia protein (PML) and the t(15;17)-generated PML-retinoic acid receptor alpha oncoprotein". Molecular and Cellular Biology. 20 (17): 6276–86. doi:10.1128/mcb.20.17.6276-6286.2000. PMC 86102. PMID 10938104.
^ ^a ^b ^c ^d ^e Khan MM, Nomura T, Kim H, Kaul SC, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi PP, Ishii S (juni 2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Molecular Cell. 7 (6): 1233–43. doi:10.1016/s1097-2765(01)00257-x. PMID 11430826.
^ ^a ^b Wu WS, Vallian S, Seto E, Yang WM, Edmondson D, Roth S, Chang KS (april 2001). "The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases". Molecular and Cellular Biology. 21 (7): 2259–68. doi:10.1128/MCB.21.7.2259-2268.2001. PMC 86860. PMID 11259576.
^ Topcu Z, Mack DL, Hromas RA, Borden KL (novembar 1999). "The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control". Oncogene. 18 (50): 7091–100. doi:10.1038/sj.onc.1203201. PMID 10597310.
^ Shin J, Park B, Cho S, Lee S, Kim Y, Lee SO, Cho K, Lee S, Jin BS, Ahn JH, Choi EJ, Ahn K (septembar 2004). "Promyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinase". The Journal of Biological Chemistry. 279 (39): 40994–1003. doi:10.1074/jbc.M407369200. PMID 15273249.
^ Dahle Ø, Bakke O, Gabrielsen OS (juli 2004). "c-Myb associates with PML in nuclear bodies in hematopoietic cells". Experimental Cell Research. 297 (1): 118–26. doi:10.1016/j.yexcr.2004.03.014. PMID 15194430.
^ ^a ^b Kurki S, Latonen L, Laiho M (oktobar 2003). "Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization". Journal of Cell Science. 116 (Pt 19): 3917–25. doi:10.1242/jcs.00714. PMID 12915590.
^ ^a ^b Bernardi R, Scaglioni PP, Bergmann S, Horn HF, Vousden KH, Pandolfi PP (juli 2004). "PML regulates p53 stability by sequestering Mdm2 to the nucleolus". Nature Cell Biology. 6 (7): 665–72. doi:10.1038/ncb1147. PMID 15195100.
^ Zhu H, Wu L, Maki CG (decembar 2003). "MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53". The Journal of Biological Chemistry. 278 (49): 49286–92. doi:10.1074/jbc.M308302200. PMID 14507915.
^ Wei X, Yu ZK, Ramalingam A, Grossman SR, Yu JH, Bloch DB, Maki CG (august 2003). "Physical and functional interactions between PML and MDM2". The Journal of Biological Chemistry. 278 (31): 29288–97. doi:10.1074/jbc.M212215200. PMID 12759344.
^ Wu WS, Xu ZX, Ran R, Meng F, Chang KS (maj 2002). "Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions". Oncogene. 21 (24): 3925–33. doi:10.1038/sj.onc.1205491. PMID 12032831.
^ Hong SH, Yang Z, Privalsky ML (novembar 2001). "Arsenic trioxide is a potent inhibitor of the interaction of SMRT corepressor with Its transcription factor partners, including the PML-retinoic acid receptor alpha oncoprotein found in human acute promyelocytic leukemia". Molecular and Cellular Biology. 21 (21): 7172–82. doi:10.1128/MCB.21.21.7172-7182.2001. PMC 99892. PMID 11585900.
^ Fogal V, Gostissa M, Sandy P, Zacchi P, Sternsdorf T, Jensen K, Pandolfi PP, Will H, Schneider C, Del Sal G (novembar 2000). "Regulation of p53 activity in nuclear bodies by a specific PML isoform". The EMBO Journal. 19 (22): 6185–95. doi:10.1093/emboj/19.22.6185. PMC 305840. PMID 11080164.
^ Guo A, Salomoni P, Luo J, Shih A, Zhong S, Gu W, Pandolfi PP (oktobar 2000). "The function of PML in p53-dependent apoptosis". Nature Cell Biology. 2 (10): 730–6. doi:10.1038/35036365. PMID 11025664.
^ Alcalay M, Tomassoni L, Colombo E, Stoldt S, Grignani F, Fagioli M, Szekely L, Helin K, Pelicci PG (februar 1998). "The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein". Molecular and Cellular Biology. 18 (2): 1084–93. doi:10.1128/mcb.18.2.1084. PMC 108821. PMID 9448006.
^ Kawasaki A, Matsumura I, Kataoka Y, Takigawa E, Nakajima K, Kanakura Y (maj 2003). "Opposing effects of PML and PML/RAR alpha on STAT3 activity". Blood. 101 (9): 3668–73. doi:10.1182/blood-2002-08-2474. PMID 12506013.
^ Lin DY, Shih HM (juli 2002). "Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration". The Journal of Biological Chemistry. 277 (28): 25446–56. doi:10.1074/jbc.M200633200. PMID 11948183.
^ Kamitani T, Nguyen HP, Kito K, Fukuda-Kamitani T, Yeh ET (februar 1998). "Covalent modification of PML by the sentrin family of ubiquitin-like proteins". The Journal of Biological Chemistry. 273 (6): 3117–20. doi:10.1074/jbc.273.6.3117. PMID 9452416.
^ Vallian S, Chin KV, Chang KS (decembar 1998). "The promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter". Molecular and Cellular Biology. 18 (12): 7147–56. doi:10.1128/MCB.18.12.7147. PMC 109296. PMID 9819401.
^ Xu ZX, Timanova-Atanasova A, Zhao RX, Chang KS (juni 2003). "PML colocalizes with and stabilizes the DNA damage response protein TopBP1". Molecular and Cellular Biology. 23 (12): 4247–56. doi:10.1128/mcb.23.12.4247-4256.2003. PMC 156140. PMID 12773567.
^ Takahashi H, Hatakeyama S, Saitoh H, Nakayama KI (februar 2005). "Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein". The Journal of Biological Chemistry. 280 (7): 5611–21. doi:10.1074/jbc.M408130200. PMID 15569683.
^ Koken MH, Reid A, Quignon F, Chelbi-Alix MK, Davies JM, Kabarowski JH, Zhu J, Dong S, Chen S, Chen Z, Tan CC, Licht J, Waxman S, de Thé H, Zelent A (septembar 1997). "Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies". Proceedings of the National Academy of Sciences of the United States of America. 94 (19): 10255–60. doi:10.1073/pnas.94.19.10255. PMC 23349. PMID 9294197.
^ ^a ^b ^c Miki T, Zhao Z, Lee CC (juli 2016). "Interactive Organization of the Circadian Core Regulators PER2, BMAL1, CLOCK and PML". Scientific Reports. 6: 29174. doi:10.1038/srep29174. PMC 4935866. PMID 27383066.

Dopunska literatura

Zhong S, Salomoni P, Pandolfi PP (maj 2000). "The transcriptional role of PML and the nuclear body". Nature Cell Biology. 2 (5): E85–90. doi:10.1038/35010583. PMID 10806494.
Jensen K, Shiels C, Freemont PS (oktobar 2001). "PML protein isoforms and the RBCC/TRIM motif". Oncogene. 20 (49): 7223–33. doi:10.1038/sj.onc.1204765. PMID 11704850.
Pearson M, Pelicci PG (oktobar 2001). "PML interaction with p53 and its role in apoptosis and replicative senescence". Oncogene. 20 (49): 7250–6. doi:10.1038/sj.onc.1204856. PMID 11704853.
Salomoni P, Pandolfi PP (januar 2002). "The role of PML in tumor suppression". Cell. 108 (2): 165–70. doi:10.1016/S0092-8674(02)00626-8. PMID 11832207.
Combes R, Balls M, Bansil L, Barratt M, Bell D, Botham P, Broadhead C, Clothier R, George E, Fentem J, Jackson M, Indans I, Loizu G, Navaratnam V, Pentreath V, Phillips B, Stemplewski H, Stewart J (2002). "An assessment of progress in the use of alternatives in toxicity testing since the publication of the report of the second FRAME Toxicity Committee (1991)". Alternatives to Laboratory Animals. 30 (4): 365–406. doi:10.1177/026119290203000403. PMID 12234245.
Bernardi R, Pandolfi PP (decembar 2003). "Role of PML and the PML-nuclear body in the control of programmed cell death". Oncogene. 22 (56): 9048–57. doi:10.1038/sj.onc.1207106. PMID 14663483.
Beez S, Demmer P, Puccetti E (2012). "Targeting the acute promyelocytic leukemia-associated fusion proteins PML/RARα and PLZF/RARα with interfering peptides". PLOS ONE. 7 (11): e48636. doi:10.1371/journal.pone.0048636. PMC 3494703. PMID 23152790.

Vanjski linkovi

PML protein, human na US National Library of Medicine Medical Subject Headings (MeSH)

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000140464 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000036986 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[Bernardi_2007-5] ^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k ^l ^m ⁿ ^o ^p ^q ^r ^s ^t ^u Bernardi R, Pandolfi PP (decembar 2007). "Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies". Nature Reviews. Molecular Cell Biology. 8 (12): 1006–16. doi:10.1038/nrm2277. PMID 17928811.

[Sahin_2014-6] Sahin U, Lallemand-Breitenbach V, de Thé H (novembar 2014). "PML nuclear bodies: regulation, function and therapeutic perspectives". The Journal of Pathology (jezik: engleski). 234 (3): 289–91. doi:10.1002/path.4426. PMID 25138686.

[UniProt-7] "UniProt, P29590". Pristupljeno 16. 7. 2021.

[8] "PML promyelocytic leukemia [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Pristupljeno 6. 12. 2016.

[Pearson_2001-9] Pearson M, Pelicci PG (2001). "PML interaction with p53 and its role in apoptosis and replicative senescence". Oncogene. 20 (49): 7250–6. doi:10.1038/sj.onc.1204856. PMID 11704853.

[10] Tang MK, Liang YJ, Chan JY, Wong SW, Chen E, Yao Y, Gan J, Xiao L, Leung HC, Kung HF, Wang H, Lee KK (21. 3. 2013). "Promyelocytic leukemia (PML) protein plays important roles in regulating cell adhesion, morphology, proliferation and migration". PLOS ONE. 8 (3): e59477. doi:10.1371/journal.pone.0059477. PMC 3605454. PMID 23555679.

[Zhou_2014-11] Zhou W, Bao S (mart 2014). "PML-mediated signaling and its role in cancer stem cells". Oncogene (jezik: engleski). 33 (12): 1475–84. doi:10.1038/onc.2013.111. PMID 23563177.

[12] Ching RW, Dellaire G, Eskiw CH, Bazett-Jones DP (mart 2005). "PML bodies: a meeting place for genomic loci?". Journal of Cell Science (jezik: engleski). 118 (Pt 5): 847–54. doi:10.1242/jcs.01700. PMID 15731002.

[Dellaire_2004-13] Dellaire G, Bazett-Jones DP (septembar 2004). "PML nuclear bodies: dynamic sensors of DNA damage and cellular stress". BioEssays (jezik: engleski). 26 (9): 963–77. doi:10.1002/bies.20089. PMID 15351967.

[Gurrieri_2004-14] Gurrieri C, Capodieci P, Bernardi R, Scaglioni PP, Nafa K, Rush LJ, Verbel DA, Cordon-Cardo C, Pandolfi PP (februar 2004). "Loss of the tumor suppressor PML in human cancers of multiple histologic origins". Journal of the National Cancer Institute (jezik: engleski). 96 (4): 269–79. doi:10.1093/jnci/djh043. PMID 14970276.

[pmid15136035-15] Kojic S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, Valle G, Faulkner G (maj 2004). "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle". Journal of Molecular Biology. 339 (2): 313–25. doi:10.1016/j.jmb.2004.03.071. PMID 15136035.

[pmid10610177-16] Zhong S, Delva L, Rachez C, Cenciarelli C, Gandini D, Zhang H, Kalantry S, Freedman LP, Pandolfi PP (novembar 1999). "A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins". Nature Genetics. 23 (3): 287–95. doi:10.1038/15463. PMID 10610177.

[pmid12622724-17] Matsuzaki K, Minami T, Tojo M, Honda Y, Saitoh N, Nagahiro S, Saya H, Nakao M (mart 2003). "PML-nuclear bodies are involved in cellular serum response". Genes to Cells. 8 (3): 275–86. doi:10.1046/j.1365-2443.2003.00632.x. PMID 12622724.

[pmid10077561-18] Doucas V, Tini M, Egan DA, Evans RM (mart 1999). "Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling". Proceedings of the National Academy of Sciences of the United States of America. 96 (6): 2627–32. doi:10.1073/pnas.96.6.2627. PMC 15819. PMID 10077561.

[pmid12727882-19] Marcello A, Ferrari A, Pellegrini V, Pegoraro G, Lusic M, Beltram F, Giacca M (maj 2003). "Recruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML protein". The EMBO Journal. 22 (9): 2156–66. doi:10.1093/emboj/cdg205. PMC 156077. PMID 12727882.

[pmid10525530-20] Ishov AM, Sotnikov AG, Negorev D, Vladimirova OV, Neff N, Kamitani T, Yeh ET, Strauss JF, Maul GG (oktobar 1999). "PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1". The Journal of Cell Biology. 147 (2): 221–34. doi:10.1083/jcb.147.2.221. PMC 2174231. PMID 10525530.

[pmid10669754-21] Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD (mart 2000). "Sequestration and inhibition of Daxx-mediated transcriptional repression by PML". Molecular and Cellular Biology. 20 (5): 1784–96. doi:10.1128/mcb.20.5.1784-1796.2000. PMC 85360. PMID 10669754.

[pmid11244500-22] Lehembre F, Müller S, Pandolfi PP, Dejean A (januar 2001). "Regulation of Pax3 transcriptional activity by SUMO-1-modified PML". Oncogene. 20 (1): 1–9. doi:10.1038/sj.onc.1204063. PMID 11244500.

[pmid10684855-23] Zhong S, Salomoni P, Ronchetti S, Guo A, Ruggero D, Pandolfi PP (februar 2000). "Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis". The Journal of Experimental Medicine. 191 (4): 631–40. doi:10.1084/jem.191.4.631. PMC 2195846. PMID 10684855.

[pmid10938104-24] Tsuzuki S, Towatari M, Saito H, Enver T (septembar 2000). "Potentiation of GATA-2 activity through interactions with the promyelocytic leukemia protein (PML) and the t(15;17)-generated PML-retinoic acid receptor alpha oncoprotein". Molecular and Cellular Biology. 20 (17): 6276–86. doi:10.1128/mcb.20.17.6276-6286.2000. PMC 86102. PMID 10938104.

[pmid11430826-25] Khan MM, Nomura T, Kim H, Kaul SC, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi PP, Ishii S (juni 2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Molecular Cell. 7 (6): 1233–43. doi:10.1016/s1097-2765(01)00257-x. PMID 11430826.

[pmid11259576-26] Wu WS, Vallian S, Seto E, Yang WM, Edmondson D, Roth S, Chang KS (april 2001). "The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases". Molecular and Cellular Biology. 21 (7): 2259–68. doi:10.1128/MCB.21.7.2259-2268.2001. PMC 86860. PMID 11259576.

[pmid10597310-27] Topcu Z, Mack DL, Hromas RA, Borden KL (novembar 1999). "The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control". Oncogene. 18 (50): 7091–100. doi:10.1038/sj.onc.1203201. PMID 10597310.

[pmid15273249-28] Shin J, Park B, Cho S, Lee S, Kim Y, Lee SO, Cho K, Lee S, Jin BS, Ahn JH, Choi EJ, Ahn K (septembar 2004). "Promyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinase". The Journal of Biological Chemistry. 279 (39): 40994–1003. doi:10.1074/jbc.M407369200. PMID 15273249.

[pmid15194430-29] Dahle Ø, Bakke O, Gabrielsen OS (juli 2004). "c-Myb associates with PML in nuclear bodies in hematopoietic cells". Experimental Cell Research. 297 (1): 118–26. doi:10.1016/j.yexcr.2004.03.014. PMID 15194430.

[pmid12915590-30] Kurki S, Latonen L, Laiho M (oktobar 2003). "Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization". Journal of Cell Science. 116 (Pt 19): 3917–25. doi:10.1242/jcs.00714. PMID 12915590.

[pmid15195100-31] Bernardi R, Scaglioni PP, Bergmann S, Horn HF, Vousden KH, Pandolfi PP (juli 2004). "PML regulates p53 stability by sequestering Mdm2 to the nucleolus". Nature Cell Biology. 6 (7): 665–72. doi:10.1038/ncb1147. PMID 15195100.

[pmid14507915-32] Zhu H, Wu L, Maki CG (decembar 2003). "MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53". The Journal of Biological Chemistry. 278 (49): 49286–92. doi:10.1074/jbc.M308302200. PMID 14507915.

[pmid12759344-33] Wei X, Yu ZK, Ramalingam A, Grossman SR, Yu JH, Bloch DB, Maki CG (august 2003). "Physical and functional interactions between PML and MDM2". The Journal of Biological Chemistry. 278 (31): 29288–97. doi:10.1074/jbc.M212215200. PMID 12759344.

[pmid12032831-34] Wu WS, Xu ZX, Ran R, Meng F, Chang KS (maj 2002). "Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions". Oncogene. 21 (24): 3925–33. doi:10.1038/sj.onc.1205491. PMID 12032831.

[pmid11585900-35] Hong SH, Yang Z, Privalsky ML (novembar 2001). "Arsenic trioxide is a potent inhibitor of the interaction of SMRT corepressor with Its transcription factor partners, including the PML-retinoic acid receptor alpha oncoprotein found in human acute promyelocytic leukemia". Molecular and Cellular Biology. 21 (21): 7172–82. doi:10.1128/MCB.21.21.7172-7182.2001. PMC 99892. PMID 11585900.

[pmid11080164-36] Fogal V, Gostissa M, Sandy P, Zacchi P, Sternsdorf T, Jensen K, Pandolfi PP, Will H, Schneider C, Del Sal G (novembar 2000). "Regulation of p53 activity in nuclear bodies by a specific PML isoform". The EMBO Journal. 19 (22): 6185–95. doi:10.1093/emboj/19.22.6185. PMC 305840. PMID 11080164.

[pmid11025664-37] Guo A, Salomoni P, Luo J, Shih A, Zhong S, Gu W, Pandolfi PP (oktobar 2000). "The function of PML in p53-dependent apoptosis". Nature Cell Biology. 2 (10): 730–6. doi:10.1038/35036365. PMID 11025664.

[pmid9448006-38] Alcalay M, Tomassoni L, Colombo E, Stoldt S, Grignani F, Fagioli M, Szekely L, Helin K, Pelicci PG (februar 1998). "The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein". Molecular and Cellular Biology. 18 (2): 1084–93. doi:10.1128/mcb.18.2.1084. PMC 108821. PMID 9448006.

[pmid12506013-39] Kawasaki A, Matsumura I, Kataoka Y, Takigawa E, Nakajima K, Kanakura Y (maj 2003). "Opposing effects of PML and PML/RAR alpha on STAT3 activity". Blood. 101 (9): 3668–73. doi:10.1182/blood-2002-08-2474. PMID 12506013.

[pmid11948183-40] Lin DY, Shih HM (juli 2002). "Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration". The Journal of Biological Chemistry. 277 (28): 25446–56. doi:10.1074/jbc.M200633200. PMID 11948183.

[pmid9452416-41] Kamitani T, Nguyen HP, Kito K, Fukuda-Kamitani T, Yeh ET (februar 1998). "Covalent modification of PML by the sentrin family of ubiquitin-like proteins". The Journal of Biological Chemistry. 273 (6): 3117–20. doi:10.1074/jbc.273.6.3117. PMID 9452416.

[pmid9819401-42] Vallian S, Chin KV, Chang KS (decembar 1998). "The promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter". Molecular and Cellular Biology. 18 (12): 7147–56. doi:10.1128/MCB.18.12.7147. PMC 109296. PMID 9819401.

[pmid12773567-43] Xu ZX, Timanova-Atanasova A, Zhao RX, Chang KS (juni 2003). "PML colocalizes with and stabilizes the DNA damage response protein TopBP1". Molecular and Cellular Biology. 23 (12): 4247–56. doi:10.1128/mcb.23.12.4247-4256.2003. PMC 156140. PMID 12773567.

[pmid15569683-44] Takahashi H, Hatakeyama S, Saitoh H, Nakayama KI (februar 2005). "Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein". The Journal of Biological Chemistry. 280 (7): 5611–21. doi:10.1074/jbc.M408130200. PMID 15569683.

[pmid9294197-45] Koken MH, Reid A, Quignon F, Chelbi-Alix MK, Davies JM, Kabarowski JH, Zhu J, Dong S, Chen S, Chen Z, Tan CC, Licht J, Waxman S, de Thé H, Zelent A (septembar 1997). "Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies". Proceedings of the National Academy of Sciences of the United States of America. 94 (19): 10255–60. doi:10.1073/pnas.94.19.10255. PMC 23349. PMID 9294197.

[pmid27383066-46] Miki T, Zhao Z, Lee CC (juli 2016). "Interactive Organization of the Circadian Core Regulators PER2, BMAL1, CLOCK and PML". Scientific Reports. 6: 29174. doi:10.1038/srep29174. PMC 4935866. PMID 27383066.

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