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10.1021/acs.nanolett.6b02995 http://scihub22266oqcxt.onion/10.1021/acs.nanolett.6b02995 C5330949!5330949!27559755     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27559755&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 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nano+Lett 2016 ; 16 (9): 5951-61 Nephropedia Template TP {{tp|p=27559755|t=2016. Mechanosensing Controlled Directly by Tyrosine Kinases |pdf=|usr=}}{{27559755}} gab.com Text Mechanosensing Controlled Directly by Tyrosine Kinases JO: Nano Lett http://www.kidney.de/pget.php?&tw=1&pmid=27559755 #FOAvip To understand how cells form tissues, we need to understand how the tyrosine kinases are involved in controlling cell mechanics, whether they act directly as parts of mechanosensing machines or indirectly. Cells test the critical parameter of matrix rigidity by locally contracting (?pinching?) matrices and measuring forces, and the depletion of contractile units causes transformation. We report here that knocking down the receptor tyrosine kinases (RTKs), AXL, and ROR2, alters rigidity sensing and increases the magnitude or duration of local contraction events, respectively. Phospho-AXL and ROR2 localize to contraction units and bind major contractile components, tropomyosin 2.1 (AXL), myosin IIA (AXL), and filamin A (ROR2). At a molecular level, phosphorylated AXL localizes to active myosin filaments and phosphorylates tropomyosin at a tyrosine critical for adhesion formation. ROR2 binding of ligand is unnecessary, but binding filamin A helps function. Thus, AXL and ROR2 alter rigidity sensing and consequently morphogenic processes by directly controlling local mechanosensory contractions without ligands. Twit Text FOAVip Mechanosensing Controlled Directly by Tyrosine Kinases ????Nano Lett http://www.kidney.de/pget.php?&tw=1&pmid=27559755 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27559755 #FOAvip English Wikipedia <ref>{{Cite pmid|27559755}}</ref> Mechanosensing Controlled Directly by Tyrosine Kinases #MMPMID27559755 Yang B; Lieu ZZ; Wolfenson H; Hameed FM; Bershadsky AD; Sheetz MP Nano Lett 2016[Sep]; 16 (9): 5951-61 PMID27559755show ga To understand how cells form tissues, we need to understand how the tyrosine kinases are involved in controlling cell mechanics, whether they act directly as parts of mechanosensing machines or indirectly. Cells test the critical parameter of matrix rigidity by locally contracting (?pinching?) matrices and measuring forces, and the depletion of contractile units causes transformation. We report here that knocking down the receptor tyrosine kinases (RTKs), AXL, and ROR2, alters rigidity sensing and increases the magnitude or duration of local contraction events, respectively. Phospho-AXL and ROR2 localize to contraction units and bind major contractile components, tropomyosin 2.1 (AXL), myosin IIA (AXL), and filamin A (ROR2). At a molecular level, phosphorylated AXL localizes to active myosin filaments and phosphorylates tropomyosin at a tyrosine critical for adhesion formation. ROR2 binding of ligand is unnecessary, but binding filamin A helps function. Thus, AXL and ROR2 alter rigidity sensing and consequently morphogenic processes by directly controlling local mechanosensory contractions without ligands. äMechanosensing Controlled Directly by Tyrosine Kinases (epmc).pdf DeepDyve Pubget Overpricing