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10.1073/pnas.1708427114 http://scihub22266oqcxt.onion/10.1073/pnas.1708427114 C5576826!5576826 !28784805     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28784805 &cmd=llinks): Failed to open stream: HTTP request failed! 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Histone phosphorylation by TRPM6 s cleaved kinase attenuates adjacent arginine methylation to regulate gene expression |pdf=|usr=}}{{28784805 }} gab.com Text Histone phosphorylation by TRPM6 s cleaved kinase attenuates adjacent arginine methylation to regulate gene expression JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28784805 #FOAvip TRPM6 and TRPM7 are members of the melastatin-related transient receptor potential (TRPM) subfamily of ion channels. Deletion of either gene in mice is embryonically lethal. TRPM6/7 are the only known examples of single polypeptides containing both an ion channel pore and a serine/threonine kinase (chanzyme). Here we show that the C-terminal kinase domain of TRPM6 is cleaved from the channel domain in a cell type-specific fashion and is active. Cleavage requires that the channel conductance is functional. The cleaved kinase translocates to the nucleus, where it is strictly localized and phosphorylates specific histone serine and threonine (S/T) residues. TRPM6-cleaved kinases (M6CKs) bind subunits of the protein arginine methyltransferase 5 (PRMT5) molecular complex that make important epigenetic modifications by methylating histone arginine residues. Histone phosphorylation by M6CK results in a dramatic decrease in methylation of arginines adjacent to M6CK-phosphorylated amino acids. Knockout of TRPM6 or inactivation of its kinase results in global changes in histone S/T phosphorylation and changes the transcription of hundreds of genes. We hypothesize that M6CK associates with the PRMT5 molecular complex in the nucleus, directing M6CK to a specific genomic location and providing site-specific histone phosphorylation. M6CK histone phosphorylation, in turn, regulates transcription by attenuating the effect of local arginine methylation. Twit Text FOAVip Histone phosphorylation by TRPM6 s cleaved kinase attenuates adjacent arginine methylation to regulate gene expression ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28784805 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28784805 #FOAvip English Wikipedia <ref>{{Cite pmid|28784805 }}</ref> Histone phosphorylation by TRPM6 s cleaved kinase attenuates adjacent arginine methylation to regulate gene expression #MMPMID28784805 Krapivinsky G ; Krapivinsky L ; Renthal NE ; Santa-Cruz A ; Manasian Y ; Clapham DE Proc Natl Acad Sci U S A 2017[Aug]; 114 (34 ): E7092-E7100 PMID28784805 show ga TRPM6 and TRPM7 are members of the melastatin-related transient receptor potential (TRPM) subfamily of ion channels. Deletion of either gene in mice is embryonically lethal. TRPM6/7 are the only known examples of single polypeptides containing both an ion channel pore and a serine/threonine kinase (chanzyme). Here we show that the C-terminal kinase domain of TRPM6 is cleaved from the channel domain in a cell type-specific fashion and is active. Cleavage requires that the channel conductance is functional. The cleaved kinase translocates to the nucleus, where it is strictly localized and phosphorylates specific histone serine and threonine (S/T) residues. TRPM6-cleaved kinases (M6CKs) bind subunits of the protein arginine methyltransferase 5 (PRMT5) molecular complex that make important epigenetic modifications by methylating histone arginine residues. Histone phosphorylation by M6CK results in a dramatic decrease in methylation of arginines adjacent to M6CK-phosphorylated amino acids. Knockout of TRPM6 or inactivation of its kinase results in global changes in histone S/T phosphorylation and changes the transcription of hundreds of genes. We hypothesize that M6CK associates with the PRMT5 molecular complex in the nucleus, directing M6CK to a specific genomic location and providing site-specific histone phosphorylation. M6CK histone phosphorylation, in turn, regulates transcription by attenuating the effect of local arginine methylation. |*Gene Expression Regulation [MESH] |Arginine/chemistry/genetics/*metabolism [MESH] |Cell Line [MESH] |Histones/chemistry/genetics/*metabolism [MESH] |Humans [MESH] |Methylation [MESH] |Phosphorylation [MESH] |Protein Domains [MESH] |Serine/genetics/metabolism [MESH] |TRPM Cation Channels/chemistry/genetics/*metabolism [MESH]Histone phosphorylation by TRPM6 s cleaved kinase attenuates adjacent (epmc).pdf DeepDyve Pubget Overpricing