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10.1021/bi101963h http://scihub22266oqcxt.onion/10.1021/bi101963h C3062375!3062375 !21280599     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=21280599 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Biochemistry 2011 ; 50 (12 ): 2187-93 Nephropedia Template TP {{tp|p=21280599 |t=2011. Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the induction of an ?-helix |pdf=|usr=}}{{21280599 }} gab.com Text Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the induction of an -helix JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=21280599 #FOAvip TRPM7 is an unusual bifunctional protein consisting of an ?-kinase domain fused to a TRP ion channel. Previously, we have identified annexin A1 as a substrate for TRPM7 kinase and found that TRPM7 phosphorylates annexin A1 at Ser5 within the N-terminal ?-helix. Annexin A1 is a Ca(2+)-dependent membrane binding protein, which has been implicated in membrane trafficking and reorganization. The N-terminal tail of annexin A1 can interact with either membranes or S100A11 protein, and it adopts the conformation of an amphipathic ?-helix upon these interactions. Moreover, the existing evidence indicates that the formation of an ?-helix is essential for these interactions. Here we show that phosphorylation at Ser5 prevents the N-terminal peptide of annexin A1 from adopting an ?-helical conformation in the presence of membrane-mimetic micelles as well as phospholipid vesicles. We also show that phosphorylation at Ser5 dramatically weakens the binding of the peptide to S100A11. Our data suggest that phosphorylation at Ser5 regulates the interaction of annexin A1 with membranes as well as S100A11 protein. Twit Text FOAVip Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the induction of an -helix ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=21280599 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21280599 #FOAvip English Wikipedia <ref>{{Cite pmid|21280599 }}</ref> Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the induction of an ?-helix #MMPMID21280599 Dorovkov MV ; Kostyukova AS ; Ryazanov AG Biochemistry 2011[Mar]; 50 (12 ): 2187-93 PMID21280599 show ga TRPM7 is an unusual bifunctional protein consisting of an ?-kinase domain fused to a TRP ion channel. Previously, we have identified annexin A1 as a substrate for TRPM7 kinase and found that TRPM7 phosphorylates annexin A1 at Ser5 within the N-terminal ?-helix. Annexin A1 is a Ca(2+)-dependent membrane binding protein, which has been implicated in membrane trafficking and reorganization. The N-terminal tail of annexin A1 can interact with either membranes or S100A11 protein, and it adopts the conformation of an amphipathic ?-helix upon these interactions. Moreover, the existing evidence indicates that the formation of an ?-helix is essential for these interactions. Here we show that phosphorylation at Ser5 prevents the N-terminal peptide of annexin A1 from adopting an ?-helical conformation in the presence of membrane-mimetic micelles as well as phospholipid vesicles. We also show that phosphorylation at Ser5 dramatically weakens the binding of the peptide to S100A11. Our data suggest that phosphorylation at Ser5 regulates the interaction of annexin A1 with membranes as well as S100A11 protein. |Amino Acid Sequence [MESH] |Animals [MESH] |Annexin A1/*chemistry/*metabolism [MESH] |Cell Membrane/metabolism [MESH] |Molecular Sequence Data [MESH] |Peptide Fragments/chemistry/metabolism [MESH] |Phosphorylation [MESH] |Protein Structure, Secondary [MESH] |S100 Proteins/metabolism [MESH] |Serine [MESH]Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the(epmc).pdf DeepDyve Pubget Overpricing