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10.7554/eLife.23172 http://scihub22266oqcxt.onion/10.7554/eLife.23172 C5376188!5376188 !28362576     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28362576 &cmd=llinks): Failed to open stream: HTTP request failed! 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Ambra1 spatially regulates Src activity and Src/FAK-mediated cancer cell invasion via trafficking networks |pdf=|usr=}}{{28362576 }} gab.com Text Ambra1 spatially regulates Src activity and Src/FAK-mediated cancer cell invasion via trafficking networks JO: Elife http://www.kidney.de/pget.php?&tw=1&pmid=28362576 #FOAvip Here, using mouse squamous cell carcinoma cells, we report a completely new function for the autophagy protein Ambra1 as the first described 'spatial rheostat' controlling the Src/FAK pathway. Ambra1 regulates the targeting of active phospho-Src away from focal adhesions into autophagic structures that cancer cells use to survive adhesion stress. Ambra1 binds to both FAK and Src in cancer cells. When FAK is present, Ambra1 is recruited to focal adhesions, promoting FAK-regulated cancer cell direction-sensing and invasion. However, when Ambra1 cannot bind to FAK, abnormally high levels of phospho-Src and phospho-FAK accumulate at focal adhesions, positively regulating adhesion and invasive migration. Spatial control of active Src requires the trafficking proteins Dynactin one and IFITM3, which we identified as Ambra1 binding partners by interaction proteomics. We conclude that Ambra1 is a core component of an intracellular trafficking network linked to tight spatial control of active Src and FAK levels, and so crucially regulates their cancer-associated biological outputs. Twit Text FOAVip Ambra1 spatially regulates Src activity and Src/FAK-mediated cancer cell invasion via trafficking networks ????Elife http://www.kidney.de/pget.php?&tw=1&pmid=28362576 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28362576 #FOAvip English Wikipedia <ref>{{Cite pmid|28362576 }}</ref> Ambra1 spatially regulates Src activity and Src/FAK-mediated cancer cell invasion via trafficking networks #MMPMID28362576 Schoenherr C ; Byron A ; Sandilands E ; Paliashvili K ; Baillie GS ; Garcia-Munoz A ; Valacca C ; Cecconi F ; Serrels B ; Frame MC Elife 2017[Mar]; 6 (ä): ä PMID28362576 show ga Here, using mouse squamous cell carcinoma cells, we report a completely new function for the autophagy protein Ambra1 as the first described 'spatial rheostat' controlling the Src/FAK pathway. Ambra1 regulates the targeting of active phospho-Src away from focal adhesions into autophagic structures that cancer cells use to survive adhesion stress. Ambra1 binds to both FAK and Src in cancer cells. When FAK is present, Ambra1 is recruited to focal adhesions, promoting FAK-regulated cancer cell direction-sensing and invasion. However, when Ambra1 cannot bind to FAK, abnormally high levels of phospho-Src and phospho-FAK accumulate at focal adhesions, positively regulating adhesion and invasive migration. Spatial control of active Src requires the trafficking proteins Dynactin one and IFITM3, which we identified as Ambra1 binding partners by interaction proteomics. We conclude that Ambra1 is a core component of an intracellular trafficking network linked to tight spatial control of active Src and FAK levels, and so crucially regulates their cancer-associated biological outputs. |*Cell Adhesion [MESH] |*Cell Movement [MESH] |Adaptor Proteins, Signal Transducing/*metabolism [MESH] |Animals [MESH] |Carcinoma, Squamous Cell/*physiopathology [MESH] |Cell Line, Tumor [MESH] |Dynactin Complex/metabolism [MESH] |Focal Adhesion Kinase 1/*metabolism [MESH] |Membrane Proteins/metabolism [MESH] |Mice [MESH]Ambra1 spatially regulates Src activity and Src/FAK-mediated cancer ce(epmc).pdf DeepDyve Pubget Overpricing