前骨髄球性白血病タンパク質とは - わかりやすく解説 Weblio辞書

前骨髄球性白血病タンパク質

出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2022/08/07 05:02 UTC 版)

前骨髄球性白血病タンパク質（ぜんこつずいきゅうせいはっけつびょうタンパクしつ、英: promyelocytic leukemia protein、略称: PML）は、PML遺伝子のタンパク質産物であり、 MYL、RNF71、PP8675、TRIM19^[5]の名称でも知られる。PMLタンパク質はがん抑制タンパク質であり、PMLボディ（PML体）と呼ばれる核内構造体（英語版）の組み立てに必要とされる。PMLボディは細胞核のクロマチン間に形成される。これらの構造体は哺乳類の核に存在し、1つの核には1から30個程度存在する^[5]。PMLボディは多くの細胞調節機能を持っており、プログラム細胞死、ゲノム安定性、抗ウイルス機能、細胞分裂の制御などに関与している^[5]^[6]。PMLの変異や欠失、それに伴うこれらの過程の調節異常は、多くの種類のがんと関係している^[5]。

出典

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000140464 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036986 - Ensembl, May 2017
^ Human PubMed Reference:
^ Mouse PubMed Reference:
^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k ^l ^m ⁿ ^o ^p ^q ^r ^s ^t ^u ^v ^w “Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies”. Nature Reviews. Molecular Cell Biology 8 (12): 1006–16. (December 2007). doi:10.1038/nrm2277. PMID 17928811.
^ ^a ^b “PML nuclear bodies: regulation, function and therapeutic perspectives” (英語). The Journal of Pathology 234 (3): 289–91. (November 2014). doi:10.1002/path.4426. PMID 25138686.
^ “Effects on differentiation by the promyelocytic leukemia PML/RARalpha protein depend on the fusion of the PML protein dimerization and RARalpha DNA binding domains”. The EMBO Journal 15 (18): 4949–58. (September 1996). doi:10.1002/j.1460-2075.1996.tb00875.x. PMC 452232. PMID 8890168.
^ “PML promyelocytic leukemia [Homo sapiens (human) - Gene - NCBI]”. www.ncbi.nlm.nih.gov. 2016年12月6日閲覧。
^ ^a ^b ^c ^d ^e “PML interaction with p53 and its role in apoptosis and replicative senescence”. Oncogene 20 (49): 7250–6. (2001). doi:10.1038/sj.onc.1204856. PMID 11704853.
^ “Promyelocytic leukemia (PML) protein plays important roles in regulating cell adhesion, morphology, proliferation and migration”. PLOS ONE 8 (3): e59477. (2013-03-21). doi:10.1371/journal.pone.0059477. PMC 3605454. PMID 23555679.
^ ^a ^b “PML-mediated signaling and its role in cancer stem cells” (英語). Oncogene 33 (12): 1475–84. (March 2014). doi:10.1038/onc.2013.111. PMID 23563177.
^ “PML bodies: a meeting place for genomic loci?” (英語). Journal of Cell Science 118 (Pt 5): 847–54. (March 2005). doi:10.1242/jcs.01700. PMID 15731002.
^ ^a ^b “PML nuclear bodies: dynamic sensors of DNA damage and cellular stress” (英語). BioEssays 26 (9): 963–77. (September 2004). doi:10.1002/bies.20089. PMID 15351967.
^ ^a ^b ^c ^d “Loss of the tumor suppressor PML in human cancers of multiple histologic origins” (英語). Journal of the National Cancer Institute 96 (4): 269–79. (February 2004). doi:10.1093/jnci/djh043. PMID 14970276.
^ “The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle”. Journal of Molecular Biology 339 (2): 313–25. (May 2004). doi:10.1016/j.jmb.2004.03.071. PMID 15136035.
^ ^a ^b “A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins”. Nature Genetics 23 (3): 287–95. (November 1999). doi:10.1038/15463. PMID 10610177.
^ ^a ^b “PML-nuclear bodies are involved in cellular serum response”. Genes to Cells 8 (3): 275–86. (March 2003). doi:10.1046/j.1365-2443.2003.00632.x. PMID 12622724.
^ “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. (March 1999). doi:10.1073/pnas.96.6.2627. PMC 15819. PMID 10077561.
^ “Recruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML protein”. The EMBO Journal 22 (9): 2156–66. (May 2003). doi:10.1093/emboj/cdg205. PMC 156077. PMID 12727882.
^ “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. (October 1999). doi:10.1083/jcb.147.2.221. PMC 2174231. PMID 10525530.
^ “Sequestration and inhibition of Daxx-mediated transcriptional repression by PML”. Molecular and Cellular Biology 20 (5): 1784–96. (March 2000). doi:10.1128/mcb.20.5.1784-1796.2000. PMC 85360. PMID 10669754.
^ “Regulation of Pax3 transcriptional activity by SUMO-1-modified PML”. Oncogene 20 (1): 1–9. (January 2001). doi:10.1038/sj.onc.1204063. PMID 11244500.
^ “Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis”. The Journal of Experimental Medicine 191 (4): 631–40. (February 2000). doi:10.1084/jem.191.4.631. PMC 2195846. PMID 10684855.
^ “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. (September 2000). doi:10.1128/mcb.20.17.6276-6286.2000. PMC 86102. PMID 10938104.
^ ^a ^b ^c ^d ^e “Role of PML and PML-RARalpha in Mad-mediated transcriptional repression”. Molecular Cell 7 (6): 1233–43. (June 2001). doi:10.1016/s1097-2765(01)00257-x. PMID 11430826.
^ ^a ^b “The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases”. Molecular and Cellular Biology 21 (7): 2259–68. (April 2001). doi:10.1128/MCB.21.7.2259-2268.2001. PMC 86860. PMID 11259576.
^ “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. (November 1999). doi:10.1038/sj.onc.1203201. PMID 10597310.
^ “Promyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinase”. The Journal of Biological Chemistry 279 (39): 40994–1003. (September 2004). doi:10.1074/jbc.M407369200. PMID 15273249.
^ “c-Myb associates with PML in nuclear bodies in hematopoietic cells”. Experimental Cell Research 297 (1): 118–26. (July 2004). doi:10.1016/j.yexcr.2004.03.014. PMID 15194430.
^ ^a ^b “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. (October 2003). doi:10.1242/jcs.00714. PMID 12915590.
^ ^a ^b “PML regulates p53 stability by sequestering Mdm2 to the nucleolus”. Nature Cell Biology 6 (7): 665–72. (July 2004). doi:10.1038/ncb1147. PMID 15195100.
^ “MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53”. The Journal of Biological Chemistry 278 (49): 49286–92. (December 2003). doi:10.1074/jbc.M308302200. PMID 14507915.
^ “Physical and functional interactions between PML and MDM2”. The Journal of Biological Chemistry 278 (31): 29288–97. (August 2003). doi:10.1074/jbc.M212215200. PMID 12759344.
^ “Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions”. Oncogene 21 (24): 3925–33. (May 2002). doi:10.1038/sj.onc.1205491. PMID 12032831.
^ “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. (November 2001). doi:10.1128/MCB.21.21.7172-7182.2001. PMC 99892. PMID 11585900.
^ “Regulation of p53 activity in nuclear bodies by a specific PML isoform”. The EMBO Journal 19 (22): 6185–95. (November 2000). doi:10.1093/emboj/19.22.6185. PMC 305840. PMID 11080164.
^ “The function of PML in p53-dependent apoptosis”. Nature Cell Biology 2 (10): 730–6. (October 2000). doi:10.1038/35036365. PMID 11025664.
^ “The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein”. Molecular and Cellular Biology 18 (2): 1084–93. (February 1998). doi:10.1128/mcb.18.2.1084. PMC 108821. PMID 9448006.
^ “Opposing effects of PML and PML/RAR alpha on STAT3 activity”. Blood 101 (9): 3668–73. (May 2003). doi:10.1182/blood-2002-08-2474. PMID 12506013.
^ “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. (July 2002). doi:10.1074/jbc.M200633200. PMID 11948183.
^ “Covalent modification of PML by the sentrin family of ubiquitin-like proteins”. The Journal of Biological Chemistry 273 (6): 3117–20. (February 1998). doi:10.1074/jbc.273.6.3117. PMID 9452416.
^ “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. (December 1998). doi:10.1128/MCB.18.12.7147. PMC 109296. PMID 9819401.
^ “PML colocalizes with and stabilizes the DNA damage response protein TopBP1”. Molecular and Cellular Biology 23 (12): 4247–56. (June 2003). doi:10.1128/mcb.23.12.4247-4256.2003. PMC 156140. PMID 12773567.
^ “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. (February 2005). doi:10.1074/jbc.M408130200. PMID 15569683.
^ “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. (September 1997). doi:10.1073/pnas.94.19.10255. PMC 23349. PMID 9294197.
^ ^a ^b ^c “Interactive Organization of the Circadian Core Regulators PER2, BMAL1, CLOCK and PML”. Scientific Reports 6: 29174. (July 2016). doi:10.1038/srep29174. PMC 4935866. PMID 27383066.

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