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10.1091/mbc.E15-08-0569 http://scihub22266oqcxt.onion/10.1091/mbc.E15-08-0569 C4814216!4814216 !26864623     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26864623 &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 (7 ): 1069-84 Nephropedia Template TP {{tp|p=26864623 |t=2016. LKB1 kinase-dependent and -independent defects disrupt polarity and adhesion signaling to drive collagen remodeling during invasion |pdf=|usr=}}{{26864623 }} gab.com Text LKB1 kinase-dependent and -independent defects disrupt polarity and adhesion signaling to drive collagen remodeling during invasion JO: Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=26864623 #FOAvip LKB1 is a serine/threonine kinase and a commonly mutated gene in lung adenocarcinoma. The majority of LKB1 mutations are truncations that disrupt its kinase activity and remove its C-terminal domain (CTD). Because LKB1 inactivation drives cancer metastasis in mice and leads to aberrant cell invasion in vitro, we sought to determine how compromised LKB1 function affects lung cancer cell polarity and invasion. Using three-dimensional models, we show that LKB1 kinase activity is essential for focal adhesion kinase-mediated cell adhesion and subsequent collagen remodeling but not cell polarity. Instead, cell polarity is overseen by the kinase-independent function of its CTD and more specifically its farnesylation. This occurs through a mesenchymal-amoeboid morphological switch that signals through the Rho-GTPase RhoA. These data suggest that a combination of kinase-dependent and -independent defects by LKB1 inactivation creates a uniquely invasive cell with aberrant polarity and adhesion signaling that drives invasion into the microenvironment. Twit Text FOAVip LKB1 kinase-dependent and -independent defects disrupt polarity and adhesion signaling to drive collagen remodeling during invasion ????Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=26864623 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26864623 #FOAvip English Wikipedia <ref>{{Cite pmid|26864623 }}</ref> LKB1 kinase-dependent and -independent defects disrupt polarity and adhesion signaling to drive collagen remodeling during invasion #MMPMID26864623 Konen J ; Wilkinson S ; Lee B ; Fu H ; Zhou W ; Jiang Y ; Marcus AI Mol Biol Cell 2016[Apr]; 27 (7 ): 1069-84 PMID26864623 show ga LKB1 is a serine/threonine kinase and a commonly mutated gene in lung adenocarcinoma. The majority of LKB1 mutations are truncations that disrupt its kinase activity and remove its C-terminal domain (CTD). Because LKB1 inactivation drives cancer metastasis in mice and leads to aberrant cell invasion in vitro, we sought to determine how compromised LKB1 function affects lung cancer cell polarity and invasion. Using three-dimensional models, we show that LKB1 kinase activity is essential for focal adhesion kinase-mediated cell adhesion and subsequent collagen remodeling but not cell polarity. Instead, cell polarity is overseen by the kinase-independent function of its CTD and more specifically its farnesylation. This occurs through a mesenchymal-amoeboid morphological switch that signals through the Rho-GTPase RhoA. These data suggest that a combination of kinase-dependent and -independent defects by LKB1 inactivation creates a uniquely invasive cell with aberrant polarity and adhesion signaling that drives invasion into the microenvironment. |*Cell Adhesion [MESH] |*Cell Polarity [MESH] |*Signal Transduction [MESH] |AMP-Activated Protein Kinase Kinases [MESH] |Adenocarcinoma of Lung [MESH] |Adenocarcinoma/metabolism/*pathology [MESH] |Collagen/*metabolism [MESH] |Focal Adhesion Kinase 1 [MESH] |Humans [MESH] |Lung Neoplasms/metabolism/*pathology [MESH] |Neoplasm Invasiveness [MESH] |Protein Prenylation [MESH] |Protein Serine-Threonine Kinases/chemistry/*metabolism [MESH]LKB1 kinase-dependent and -independent defects disrupt polarity and ad(epmc).pdf DeepDyve Pubget Overpricing