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10.1681/ASN.2016040414 http://scihub22266oqcxt.onion/10.1681/ASN.2016040414 C5328162!5328162 !27628902     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27628902 &cmd=llinks): Failed to open stream: HTTP request failed! 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Synaptopodin Is a Coincidence Detector of Tyrosine versus Serine/Threonine Phosphorylation for the Modulation of Rho Protein Crosstalk in Podocytes |pdf=|usr=}}{{27628902 }} gab.com Text Synaptopodin Is a Coincidence Detector of Tyrosine versus Serine/Threonine Phosphorylation for the Modulation of Rho Protein Crosstalk in Podocytes JO: J Am Soc Nephrol http://www.kidney.de/pget.php?&tw=1&pmid=27628902 #FOAvip Tyrosine and serine/threonine signal-transduction pathways influence many aspects of cell behavior, including the spatial and temporal regulation of the actin cytoskeleton. However, little is known about how input from diverse tyrosine and serine/threonine kinases is integrated to control Rho protein crosstalk and actin remodeling, which are critically important in podocyte health and disease. Here we unveil the proteolytically-regulated, actin organizing protein synaptopodin as a coincidence detector of tyrosine versus serine/threonine phosphorylation. We show that serine/threonine and tyrosine kinases duel for synaptopodin stability versus degradation. EGFR/Src-mediated tyrosine phosphorylation of synaptopodin in podocytes promotes binding to the serine/threonine phosphatase calcineurin. This leads to the loss of 14-3-3 binding, resulting in synaptopodin degradation, Vav2 activation, enhanced Rac1 signaling, and ultimate loss of stress fibers. Our studies reveal how synaptopodin, a single proteolytically-controlled protein, integrates antagonistic tyrosine versus serine/threonine phosphorylation events for the dynamic control of the actin cytoskeleton in podocytes. Twit Text FOAVip Synaptopodin Is a Coincidence Detector of Tyrosine versus Serine/Threonine Phosphorylation for the Modulation of Rho Protein Crosstalk in Podocytes ????J Am Soc Nephrol http://www.kidney.de/pget.php?&tw=1&pmid=27628902 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27628902 #FOAvip English Wikipedia <ref>{{Cite pmid|27628902 }}</ref> Synaptopodin Is a Coincidence Detector of Tyrosine versus Serine/Threonine Phosphorylation for the Modulation of Rho Protein Crosstalk in Podocytes #MMPMID27628902 Buvall L ; Wallentin H ; Sieber J ; Andreeva S ; Choi HY ; Mundel P ; Greka A J Am Soc Nephrol 2017[Mar]; 28 (3 ): 837-851 PMID27628902 show ga Tyrosine and serine/threonine signal-transduction pathways influence many aspects of cell behavior, including the spatial and temporal regulation of the actin cytoskeleton. However, little is known about how input from diverse tyrosine and serine/threonine kinases is integrated to control Rho protein crosstalk and actin remodeling, which are critically important in podocyte health and disease. Here we unveil the proteolytically-regulated, actin organizing protein synaptopodin as a coincidence detector of tyrosine versus serine/threonine phosphorylation. We show that serine/threonine and tyrosine kinases duel for synaptopodin stability versus degradation. EGFR/Src-mediated tyrosine phosphorylation of synaptopodin in podocytes promotes binding to the serine/threonine phosphatase calcineurin. This leads to the loss of 14-3-3 binding, resulting in synaptopodin degradation, Vav2 activation, enhanced Rac1 signaling, and ultimate loss of stress fibers. Our studies reveal how synaptopodin, a single proteolytically-controlled protein, integrates antagonistic tyrosine versus serine/threonine phosphorylation events for the dynamic control of the actin cytoskeleton in podocytes. |Animals [MESH] |Calcineurin/metabolism [MESH] |Cells, Cultured [MESH] |Mice [MESH] |Microfilament Proteins/*physiology [MESH] |Phosphorylation [MESH] |Podocytes/*physiology [MESH] |Receptor Cross-Talk [MESH] |Serine/*metabolism [MESH] |Signal Transduction [MESH] |Threonine/*metabolism [MESH] |Tyrosine/*metabolism [MESH]Synaptopodin Is a Coincidence Detector of Tyrosine versus Serine/Threo(epmc).pdf DeepDyve Pubget Overpricing