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10.1091/mbc.E15-07-0527 http://scihub22266oqcxt.onion/10.1091/mbc.E15-07-0527 C4791125!4791125 !26823016     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26823016 &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       Mol+Biol+Cell 2016 ; 27 (6 ): 1040-50 Nephropedia Template TP {{tp|p=26823016 |t=2016. Regulatory roles of conserved phosphorylation sites in the activation T-loop of the MAP kinase ERK1 |pdf=|usr=}}{{26823016 }} gab.com Text Regulatory roles of conserved phosphorylation sites in the activation T-loop of the MAP kinase ERK1 JO: Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=26823016 #FOAvip The catalytic domains of most eukaryotic protein kinases are highly conserved in their primary structures. Their phosphorylation within the well-known activation T-loop, a variable region between protein kinase catalytic subdomains VII and VIII, is a common mechanism for stimulation of their phosphotransferase activities. Extracellular signal-regulated kinase 1 (ERK1), a member of the extensively studied mitogen-activated protein kinase (MAPK) family, serves as a paradigm for regulation of protein kinases in signaling modules. In addition to the well-documented T202 and Y204 stimulatory phosphorylation sites in the activation T-loop of ERK1 and its closest relative, ERK2, three additional flanking phosphosites have been confirmed (T198, T207, and Y210 from ERK1) by high-throughput mass spectrometry. In vitro kinase assays revealed the functional importance of T207 and Y210, but not T198, in negatively regulating ERK1 catalytic activity. The Y210 site could be important for proper conformational arrangement of the active site, and a Y210F mutant could not be recognized by MEK1 for phosphorylation of T202 and Y204 in vitro. Autophosphorylation of T207 reduces the catalytic activity and stability of activated ERK1. We propose that after the activation of ERK1 by MEK1, subsequent slower phosphorylation of the flanking sites results in inhibition of the kinase. Because the T207 and Y210 phosphosites of ERK1 are highly conserved within the eukaryotic protein kinase family, hyperphosphorylation within the kinase activation T-loop may serve as a general mechanism for protein kinase down-regulation after initial activation by their upstream kinases. Twit Text FOAVip Regulatory roles of conserved phosphorylation sites in the activation T-loop of the MAP kinase ERK1 ????Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=26823016 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26823016 #FOAvip English Wikipedia <ref>{{Cite pmid|26823016 }}</ref> Regulatory roles of conserved phosphorylation sites in the activation T-loop of the MAP kinase ERK1 #MMPMID26823016 Lai S ; Pelech S Mol Biol Cell 2016[Mar]; 27 (6 ): 1040-50 PMID26823016 show ga The catalytic domains of most eukaryotic protein kinases are highly conserved in their primary structures. Their phosphorylation within the well-known activation T-loop, a variable region between protein kinase catalytic subdomains VII and VIII, is a common mechanism for stimulation of their phosphotransferase activities. Extracellular signal-regulated kinase 1 (ERK1), a member of the extensively studied mitogen-activated protein kinase (MAPK) family, serves as a paradigm for regulation of protein kinases in signaling modules. In addition to the well-documented T202 and Y204 stimulatory phosphorylation sites in the activation T-loop of ERK1 and its closest relative, ERK2, three additional flanking phosphosites have been confirmed (T198, T207, and Y210 from ERK1) by high-throughput mass spectrometry. In vitro kinase assays revealed the functional importance of T207 and Y210, but not T198, in negatively regulating ERK1 catalytic activity. The Y210 site could be important for proper conformational arrangement of the active site, and a Y210F mutant could not be recognized by MEK1 for phosphorylation of T202 and Y204 in vitro. Autophosphorylation of T207 reduces the catalytic activity and stability of activated ERK1. We propose that after the activation of ERK1 by MEK1, subsequent slower phosphorylation of the flanking sites results in inhibition of the kinase. Because the T207 and Y210 phosphosites of ERK1 are highly conserved within the eukaryotic protein kinase family, hyperphosphorylation within the kinase activation T-loop may serve as a general mechanism for protein kinase down-regulation after initial activation by their upstream kinases. |*MAP Kinase Signaling System [MESH] |Animals [MESH] |Catalytic Domain [MESH] |Cell Line [MESH] |Down-Regulation [MESH] |Humans [MESH] |MAP Kinase Kinase 1/metabolism [MESH] |Mitogen-Activated Protein Kinase 3/*chemistry/genetics/*metabolism [MESH]Regulatory roles of conserved phosphorylation sites in the activation (epmc).pdf DeepDyve Pubget Overpricing