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10.7554/eLife.22759 http://scihub22266oqcxt.onion/10.7554/eLife.22759 C5400502!5400502!28430576     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2017 ; 6 (ä): ä Nephropedia Template TP {{tp|p=28430576|t=2017. Ezrin activation by LOK phosphorylation involves a PIP2-dependent wedge mechanism |pdf=|usr=}}{{28430576}} gab.com Text Ezrin activation by LOK phosphorylation involves a PIP2-dependent wedge mechanism JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=28430576 #FOAvip How cells specify morphologically distinct plasma membrane domains is poorly understood. Prior work has shown that restriction of microvilli to the apical aspect of epithelial cells requires the localized activation of the membrane-F-actin linking protein ezrin. Using an in vitro system, we now define a multi-step process whereby the kinase LOK specifically phosphorylates ezrin to activate it. Binding of PIP2 to ezrin induces a conformational change permitting the insertion of the LOK C-terminal domain to wedge apart the membrane and F-actin-binding domains of ezrin. The N-terminal LOK kinase domain can then access a site 40 residues distal from the consensus sequence that collectively direct phosphorylation of the appropriate threonine residue. We suggest that this elaborate mechanism ensures that ezrin is only phosphorylated at the plasma membrane, and with high specificity by the apically localized kinase LOK.DOI:http://dx.doi.org/10.7554/eLife.22759.001 Twit Text FOAVip Ezrin activation by LOK phosphorylation involves a PIP2-dependent wedge mechanism ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=28430576 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28430576 #FOAvip English Wikipedia <ref>{{Cite pmid|28430576}}</ref> Ezrin activation by LOK phosphorylation involves a PIP2-dependent wedge mechanism #MMPMID28430576 Pelaseyed T; Viswanatha R; Sauvanet C; Filter JJ; Goldberg ML; Bretscher A eLife 2017[]; 6 (ä): ä PMID28430576show ga How cells specify morphologically distinct plasma membrane domains is poorly understood. Prior work has shown that restriction of microvilli to the apical aspect of epithelial cells requires the localized activation of the membrane-F-actin linking protein ezrin. Using an in vitro system, we now define a multi-step process whereby the kinase LOK specifically phosphorylates ezrin to activate it. Binding of PIP2 to ezrin induces a conformational change permitting the insertion of the LOK C-terminal domain to wedge apart the membrane and F-actin-binding domains of ezrin. The N-terminal LOK kinase domain can then access a site 40 residues distal from the consensus sequence that collectively direct phosphorylation of the appropriate threonine residue. We suggest that this elaborate mechanism ensures that ezrin is only phosphorylated at the plasma membrane, and with high specificity by the apically localized kinase LOK.DOI:http://dx.doi.org/10.7554/eLife.22759.001 äEzrin activation by LOK phosphorylation involves a PIP2-dependent wedg(epmc).pdf DeepDyve Pubget Overpricing