Promyelocytic leukemia protein

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Promyelocytic leukemia

PDB rendering based on 1bor.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsPML; MYL; PP8675; RNF71; TRIM19
External IDsOMIM: 102578 MGI: 104662 HomoloGene: 13245 GeneCards: PML Gene
Orthologs
SpeciesHumanMouse
Entrez537118854
EnsemblENSG00000140464ENSMUSG00000036986
UniProtP29590Q60953
RefSeq (mRNA)NM_002675NM_008884
RefSeq (protein)NP_002666NP_032910
Location (UCSC)Chr 15:
74.29 – 74.34 Mb		Chr 9:
58.22 – 58.25 Mb
PubMed search
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Probable transcription factor PML is a tumor suppressor protein that in humans is encoded by the PML gene.

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This phosphoprotein localizes to nuclear bodies (Nuclear dots) where it functions as a transcription factor and tumor suppressor. Its expression is cell-cycle related and it regulates the p53 response to oncogenic signals. The gene is often involved in the translocation with the retinoic acid receptor alpha gene associated with acute promyelocytic leukemia (APL). Extensive alternative splicing of this gene results in several variations of the protein's central and C-terminal regions; all variants encode the same N-terminus. Alternatively spliced transcript variants encoding different isoforms have been identified.[1]

Interactions

Promyelocytic leukemia protein has been shown to interact with Retinoic acid receptor alpha,[2] HDAC1,[3][4] Nerve Growth factor IB,[5] SKI protein,[3] Zinc finger and BTB domain-containing protein 16,[6] Cyclin T1,[7] SIN3A,[3] Retinoblastoma protein,[8] Death associated protein 6,[9][10][11][12] STAT3,[13] CREB-binding protein,[2][14][15] Sp1 transcription factor,[16] ANKRD2,[17] Thymine-DNA glycosylase,[18] TOPBP1,[19] HHEX,[20] MAPK11,[21] Nuclear receptor co-repressor 1,[3] Nuclear receptor co-repressor 2,[3][22] P53,[23][24][25] MYB,[26] HDAC3,[4] GATA2,[27] RPL11,[28] Mdm2,[23][28][29][30] Serum response factor[14] and Small ubiquitin-related modifier 1.[31][32]

See also

References

  1. ↑ "Entrez Gene: PML promyelocytic leukemia". 
  2. ↑ 2.0 2.1 Zhong, S; Delva L, Rachez C, Cenciarelli C, Gandini D, Zhang H, Kalantry S, Freedman L P, Pandolfi P P (Nov 1999). "A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins". Nat. Genet. (UNITED STATES) 23 (3): 287–95. doi:10.1038/15463. ISSN 1061-4036. PMID 10610177. 
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Khan, M M; Nomura T, Kim H, Kaul S C, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi P P, Ishii S (Jun 2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Mol. Cell (United States) 7 (6): 1233–43. doi:10.1016/S1097-2765(01)00257-X. ISSN 1097-2765. PMID 11430826. 
  4. ↑ 4.0 4.1 Wu, W S; Vallian S, Seto E, Yang W M, Edmondson D, Roth S, Chang K S (Apr 2001). "The Growth Suppressor PML Represses Transcription by Functionally and Physically Interacting with Histone Deacetylases". Mol. Cell. Biol. (United States) 21 (7): 2259–68. doi:10.1128/MCB.21.7.2259-2268.2001. ISSN 0270-7306. PMC 86860. PMID 11259576. 
  5. ↑ Wu, Wen-Shu; Xu Zhi-Xiang, Ran Ruixiang, Meng Feng, Chang Kun-Sang (May 2002). "Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions". Oncogene (England) 21 (24): 3925–33. doi:10.1038/sj.onc.1205491. ISSN 0950-9232. PMID 12032831. 
  6. ↑ Koken, M H; Reid A, Quignon F, Chelbi-Alix M K, Davies J M, Kabarowski J H, Zhu J, Dong S, Chen S, Chen Z, Tan C C, Licht J, Waxman S, de Thé H, Zelent A (Sep 1997). "Leukemia-associated retinoic acid receptor α fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (19): 10255–60. doi:10.1073/pnas.94.19.10255. ISSN 0027-8424. PMC 23349. PMID 9294197. 
  7. ↑ Marcello, Alessandro; Ferrari Aldo, Pellegrini Vittorio, Pegoraro Gianluca, Lusic Marina, Beltram Fabio, Giacca Mauro (May 2003). "Recruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML protein". EMBO J. (England) 22 (9): 2156–66. doi:10.1093/emboj/cdg205. ISSN 0261-4189. PMC 156077. PMID 12727882. 
  8. ↑ Alcalay, M; Tomassoni L, Colombo E, Stoldt S, Grignani F, Fagioli M, Szekely L, Helin K, Pelicci P G (Feb 1998). "The Promyelocytic Leukemia Gene Product (PML) Forms Stable Complexes with the Retinoblastoma Protein". Mol. Cell. Biol. (UNITED STATES) 18 (2): 1084–93. ISSN 0270-7306. PMC 108821. PMID 9448006. 
  9. ↑ Ishov, A M; Sotnikov A G, Negorev D, Vladimirova O V, Neff N, Kamitani T, Yeh E T, Strauss J F, Maul G G (Oct 1999). "Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1". J. Cell Biol. (UNITED STATES) 147 (2): 221–34. doi:10.1083/jcb.147.2.221. ISSN 0021-9525. PMC 2174231. PMID 10525530. 
  10. ↑ Li, H; Leo C, Zhu J, Wu X, O'Neil J, Park E J, Chen J D (Mar 2000). "Sequestration and Inhibition of Daxx-Mediated Transcriptional Repression by PML". Mol. Cell. Biol. (UNITED STATES) 20 (5): 1784–96. doi:10.1128/MCB.20.5.1784-1796.2000. ISSN 0270-7306. PMC 85360. PMID 10669754. 
  11. ↑ Lehembre, F; Müller S, Pandolfi P P, Dejean A (Jan 2001). "Regulation of Pax3 transcriptional activity by SUMO-1-modified PML". Oncogene (England) 20 (1): 1–9. doi:10.1038/sj.onc.1204063. ISSN 0950-9232. PMID 11244500. 
  12. ↑ Zhong, S; Salomoni P, Ronchetti S, Guo A, Ruggero D, Pandolfi P P (Feb 2000). "Promyelocytic Leukemia Protein (Pml) and Daxx Participate in a Novel Nuclear Pathway for Apoptosis". J. Exp. Med. (UNITED STATES) 191 (4): 631–40. doi:10.1084/jem.191.4.631. ISSN 0022-1007. PMC 2195846. PMID 10684855. 
  13. ↑ Kawasaki, Akira; Matsumura Itaru, Kataoka Yoshihisa, Takigawa Eri, Nakajima Koichi, Kanakura Yuzuru (May 2003). "Opposing effects of PML and PML/RAR alpha on STAT3 activity". Blood (United States) 101 (9): 3668–73. doi:10.1182/blood-2002-08-2474. ISSN 0006-4971. PMID 12506013. 
  14. ↑ 14.0 14.1 Matsuzaki, Kazuhito; Minami Takeshi, Tojo Masahide, Honda Yoshiomi, Saitoh Noriko, Nagahiro Shinji, Saya Hideyuki, Nakao Mitsuyoshi (Mar 2003). "PML-nuclear bodies are involved in cellular serum response". Genes Cells (England) 8 (3): 275–86. doi:10.1046/j.1365-2443.2003.00632.x. ISSN 1356-9597. PMID 12622724. 
  15. ↑ Doucas, V; Tini M, Egan D A, Evans R M (Mar 1999). "Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (6): 2627–32. doi:10.1073/pnas.96.6.2627. ISSN 0027-8424. PMC 15819. PMID 10077561. 
  16. ↑ Vallian, S; Chin K V, Chang K S (Dec 1998). "The Promyelocytic Leukemia Protein Interacts with Sp1 and Inhibits Its Transactivation of the Epidermal Growth Factor Receptor Promoter". Mol. Cell. Biol. (UNITED STATES) 18 (12): 7147–56. ISSN 0270-7306. PMC 109296. PMID 9819401. 
  17. ↑ Kojic, Snezana; Medeot Elisa, Guccione Ernesto, Krmac Helena, Zara Ivano, Martinelli Valentina, Valle Giorgio, Faulkner Georgine (May 2004). "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle". J. Mol. Biol. (England) 339 (2): 313–25. doi:10.1016/j.jmb.2004.03.071. ISSN 0022-2836. PMID 15136035. 
  18. ↑ Takahashi, Hidehisa; Hatakeyama Shigetsugu, Saitoh Hisato, Nakayama Keiichi I (Feb 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". J. Biol. Chem. (United States) 280 (7): 5611–21. doi:10.1074/jbc.M408130200. ISSN 0021-9258. PMID 15569683. 
  19. ↑ Xu, Zhi-Xiang; Timanova-Atanasova Anna, Zhao Rui-Xun, Chang Kun-Sang (Jun 2003). "PML Colocalizes with and Stabilizes the DNA Damage Response Protein TopBP1". Mol. Cell. Biol. (United States) 23 (12): 4247–56. doi:10.1128/MCB.23.12.4247-4256.2003. ISSN 0270-7306. PMC 156140. PMID 12773567. 
  20. ↑ Topcu, Z; Mack D L, Hromas R A, Borden K L (Nov 1999). "The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control". Oncogene (ENGLAND) 18 (50): 7091–100. doi:10.1038/sj.onc.1203201. ISSN 0950-9232. PMID 10597310. 
  21. ↑ Shin, Jinwook; Park Boyoun, Cho Sunglim, Lee Sunray, Kim Youngkyun, Lee Seong-Ok, Cho Kwangmin, Lee Sungwook, Jin Bong-Suk, Ahn Jin-Hyun, Choi Eui-Ju, Ahn Kwangseog (Sep 2004). "Promyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinase". J. Biol. Chem. (United States) 279 (39): 40994–1003. doi:10.1074/jbc.M407369200. ISSN 0021-9258. PMID 15273249. 
  22. ↑ Hong, S H; Yang Z, Privalsky M L (Nov 2001). "Arsenic Trioxide Is a Potent Inhibitor of the Interaction of SMRT Corepressor with Its Transcription Factor Partners, Including the PML-Retinoic Acid Receptor α Oncoprotein Found in Human Acute Promyelocytic Leukemia". Mol. Cell. Biol. (United States) 21 (21): 7172–82. doi:10.1128/MCB.21.21.7172-7182.2001. ISSN 0270-7306. PMC 99892. PMID 11585900. 
  23. ↑ 23.0 23.1 Kurki, Sari; Latonen Leena, Laiho Marikki (Oct 2003). "Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization". J. Cell. Sci. (England) 116 (Pt 19): 3917–25. doi:10.1242/jcs.00714. ISSN 0021-9533. PMID 12915590. 
  24. ↑ Fogal, V; Gostissa M, Sandy P, Zacchi P, Sternsdorf T, Jensen K, Pandolfi P P, Will H, Schneider C, Del Sal G (Nov 2000). "Regulation of p53 activity in nuclear bodies by a specific PML isoform". EMBO J. (ENGLAND) 19 (22): 6185–95. doi:10.1093/emboj/19.22.6185. ISSN 0261-4189. PMC 305840. PMID 11080164. 
  25. ↑ Guo, A; Salomoni P, Luo J, Shih A, Zhong S, Gu W, Pandolfi P P (Oct 2000). "The function of PML in p53-dependent apoptosis". Nat. Cell Biol. (ENGLAND) 2 (10): 730–6. doi:10.1038/35036365. ISSN 1465-7392. PMID 11025664. 
  26. ↑ Dahle, Øyvind; Bakke Oddmund, Gabrielsen Odd Stokke (Jul 2004). "c-Myb associates with PML in nuclear bodies in hematopoietic cells". Exp. Cell Res. (United States) 297 (1): 118–26. doi:10.1016/j.yexcr.2004.03.014. ISSN 0014-4827. PMID 15194430. 
  27. ↑ Tsuzuki, S; Towatari M, Saito H, Enver T (Sep 2000). "Potentiation of GATA-2 Activity through Interactions with the Promyelocytic Leukemia Protein (PML) and the t(15;17)-Generated PML-Retinoic Acid Receptor α Oncoprotein". Mol. Cell. Biol. (UNITED STATES) 20 (17): 6276–86. doi:10.1128/MCB.20.17.6276-6286.2000. ISSN 0270-7306. PMC 86102. PMID 10938104. 
  28. ↑ 28.0 28.1 Bernardi, Rosa; Scaglioni Pier Paolo, Bergmann Stephan, Horn Henning F, Vousden Karen H, Pandolfi Pier Paolo (Jul 2004). "PML regulates p53 stability by sequestering Mdm2 to the nucleolus". Nat. Cell Biol. (England) 6 (7): 665–72. doi:10.1038/ncb1147. ISSN 1465-7392. PMID 15195100. 
  29. ↑ Zhu, Hongyan; Wu Liqing, Maki Carl G (Dec 2003). "MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53". J. Biol. Chem. (United States) 278 (49): 49286–92. doi:10.1074/jbc.M308302200. ISSN 0021-9258. PMID 14507915. 
  30. ↑ Wei, Xiaolong; Yu Zhong Kang, Ramalingam Arivudainambi, Grossman Steven R, Yu Jiang H, Bloch Donald B, Maki Carl G (Aug 2003). "Physical and functional interactions between PML and MDM2". J. Biol. Chem. (United States) 278 (31): 29288–97. doi:10.1074/jbc.M212215200. ISSN 0021-9258. PMID 12759344. 
  31. ↑ Lin, Ding-Yen; Shih Hsiu-Ming (Jul 2002). "Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration". J. Biol. Chem. (United States) 277 (28): 25446–56. doi:10.1074/jbc.M200633200. ISSN 0021-9258. PMID 11948183. 
  32. ↑ Kamitani, T; Nguyen H P, Kito K, Fukuda-Kamitani T, Yeh E T (Feb 1998). "Covalent modification of PML by the sentrin family of ubiquitin-like proteins". J. Biol. Chem. (UNITED STATES) 273 (6): 3117–20. doi:10.1074/jbc.273.6.3117. ISSN 0021-9258. PMID 9452416. 

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