| 词条 | CARM1 |
| 释义 |
| Name = coactivator-associated arginine methyltransferase 1 | caption = Crystal Structure of Coactivator Associated Arginine Methyltransferase 1[1] | image = PDB1.png | width = | HGNCid = 23393 | Symbol = CARM1 | AltSymbols = | EntrezGene = 10498 | OMIM = 603934 | RefSeq = XM_032719 | UniProt = Q86X55 | PDB = | ECnumber = 2.1.1.125 | Chromosome = 19 | Arm = p | Band = 13.2 | LocusSupplementaryData = }}{{infobox protein | Name = coactivator associated arginine methyltransferase 1-like | caption = | image = | width = | HGNCid = 23392 | Symbol = CARM1L | AltSymbols = | EntrezGene = 256280 | OMIM = | RefSeq = XM_171224 | UniProt = Q5SZY8 | PDB = | ECnumber = | Chromosome = 9 | Arm = p | Band = 24.2 | LocusSupplementaryData = }}CARM1 (coactivator-associated arginine methyltransferase 1), also known as PRMT4 (protein arginine N-methyltransferase 4), is an enzyme ({{EC number|2.1.1.125}}) encoded by the {{gene|CARM1}} gene found in human beings, as well as many other mammals.[2] It has a polypeptide (L) chain type that is 348 residues long, and is made up of alpha helices and beta sheets.[3] Its main function includes catalyzing the transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine.[4] CARM1 is a secondary coactivator through its association with p160 family (SRC-1, GRIP1, AIB) of coactivators. It is responsible for moving cells toward the inner cell mass in developing blastocysts.[5] Clinical significanceCARM1 plays an important role in androgen receptors and may play a role in prostate cancer progression.[6][7] CARM1 exerts both oncogenic and tumor-suppressive functions. In breast cancer, CARM1 methylates chromatin remodeling factor BAF155 to enhance tumor progression and metastasis.[8] In pancreatic cancer, CARM1 methylates and inhibits MDH1 by disrupting its dimerization, which represses mitochondria respiration and inhibits glutamine utilization. CARM1-mediated MDH1 methylation reduces cellular NADPH level and sensitizes cells to oxidative stress, thereby suppressing cell proliferation and colony formation.[9] See also
External links
References1. ^{{cite web |url=http://www.rcsb.org/pdb/explore/explore.do?structureId=2Y1W |title=RCSB Protein Data Bank - Structure Summary for 2Y1W - CRYSTAL STRUCTURE OF COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1) IN COMPLEX WITH SINEFUNGIN AND INDOLE INHIBITOR |format= |work= |accessdate=}} {{Transcription coregulators}}{{enzyme-stub}}2. ^{{cite journal | vauthors = Chen D, Ma H, Hong H, Koh SS, Huang SM, Schurter BT, Aswad DW, Stallcup MR | title = Regulation of transcription by a protein methyltransferase | journal = Science | volume = 284 | issue = 5423 | pages = 2174–7 | year = 1999 | pmid = 10381882 | doi = 10.1126/science.284.5423.2174 }} 3. ^{{cite web |url=http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2Y1W |title=RCSB Protein Data Bank - Sequence / Structure Details for 2Y1W - CRYSTAL STRUCTURE OF COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1) IN COMPLEX WITH SINEFUNGIN AND INDOLE INHIBITOR |format= |work= |accessdate=}} 4. ^{{cite web |url=https://www.genecards.org/cgi-bin/carddisp.pl?gene=CARM1 |title=CARM1 Gene - GeneCards | CARM1 Protein | CARM1 Antibody |format= |work= |accessdate=}} 5. ^{{cite journal | vauthors = Torres-Padilla ME, Parfitt DE, Kouzarides T, Zernicka-Goetz M | title = Histone arginine methylation regulates pluripotency in the early mouse embryo | journal = Nature | volume = 445 | issue = 7124 | pages = 214–8 | year = 2007 | pmid = 17215844 | doi = 10.1038/nature05458 | pmc=3353120}} 6. ^{{cite journal | vauthors = Hong H, Kao C, Jeng MH, Eble JN, Koch MO, Gardner TA, Zhang S, Li L, Pan CX, Hu Z, MacLennan GT, Cheng L | title = Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status | journal = Cancer | volume = 101 | issue = 1 | pages = 83–9 | year = 2004 | pmid = 15221992 | doi = 10.1002/cncr.20327 }} 7. ^{{cite journal | vauthors = Majumder S, Liu Y, Ford OH, Mohler JL, Whang YE | title = Involvement of arginine methyltransferase CARM1 in androgen receptor function and prostate cancer cell viability | journal = Prostate | volume = 66 | issue = 12 | pages = 1292–301 | year = 2006 | pmid = 16705743 | doi = 10.1002/pros.20438 }} 8. ^{{cite journal | vauthors = Wang L, Zhao Z, Meyer MB, Saha S, Yu M, Guo A, Wisinski KB, Huang W, Cai W, Pike JW, Yuan M, Ahlquist P, Xu W | title = CARM1 Methylates Chromatin Remodeling Factor BAF155 to Enhance Tumor Progression and Metastasis | journal = Cancer Cell | volume = 30 | issue = 1 | pages = 179–180 | date = Jul 2016 | pmid = 27479032 | doi = 10.1016/j.ccell.2016.06.013 }} 9. ^{{cite journal | vauthors = Wang YP, Zhou W, Wang J, Huang X, Zuo Y, Wang TS, Gao X, Xu YY, Zou SW, Liu YB, Cheng JK, Lei QY | title = Arginine Methylation of MDH1 by CARM1 Inhibits Glutamine Metabolism and Suppresses Pancreatic Cancer | journal = Molecular Cell | volume = 64 | issue = 4 | pages = 673–87 | date = Nov 2016 | pmid = 27840030 | doi = 10.1016/j.molcel.2016.09.028 }} 1 : Transcription coregulators |
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