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10.1371/journal.pone.0184285 http://scihub22266oqcxt.onion/10.1371/journal.pone.0184285 C5584928!5584928 !28873464     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28873464 &cmd=llinks): Failed to open stream: HTTP request failed! 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Direct integrin binding to insulin-like growth factor-2 through the C-domain is required for insulin-like growth factor receptor type 1 (IGF1R) signaling |pdf=|usr=}}{{28873464 }} gab.com Text Direct integrin binding to insulin-like growth factor-2 through the C-domain is required for insulin-like growth factor receptor type 1 (IGF1R) signaling JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=28873464 #FOAvip We have reported that integrins crosstalk with growth factors through direct binding to growth factors (e.g., fibroblast growth factor-1, insulin-like growth factor 1 (IGF1), neuregulin-1, fractalkine) and subsequent ternary complex formation with cognate receptor [e.g., integrin/IGF1/IGF1 receptor (IGF1R)]. IGF1 and IGF2 are overexpressed in cancer and major therapeutic targets. We previously reported that IGF1 binds to integrins ???3 and ?6?4, and the R36E/R37E mutant in the C-domain of IGF1 is defective integrin binding and signaling functions of IGF1, and acts as an antagonist of IGF1R. We studied if integrins play a role in the signaling functions of IGF2, another member of the IGF family. Here we describe that IGF2 specifically binds to integrins ???3 and ?6?4, and induced proliferation of CHO cells (IGF1R+) that express ???3 or ?6?4 (?3- or ?6?4-CHO cells). Arg residues to Glu at positions 24, 34, 37 and/or 38 in or close to the C-domain of IGF2 play a critical role in binding to integrins and signaling functions. The R24E/R37E/R38E, R34E/R37E/R38E, and R24E/R34E/R37E/R38E mutants were defective in integrin binding and IGF2 signaling. These mutants suppressed proliferation induced by WT IGF2, suggesting that they are dominant-negative antagonists of IGF1R. These results suggest that IGF2 also requires integrin binding for signaling functions, and the IGF2 mutants that cannot bind to integrins act as antagonists of IGF1R. The present study defines the role of the C-domain in integrin binding and signaling. Twit Text FOAVip Direct integrin binding to insulin-like growth factor-2 through the C-domain is required for insulin-like growth factor receptor type 1 (IGF1R) signaling ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=28873464 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28873464 #FOAvip English Wikipedia <ref>{{Cite pmid|28873464 }}</ref> Direct integrin binding to insulin-like growth factor-2 through the C-domain is required for insulin-like growth factor receptor type 1 (IGF1R) signaling #MMPMID28873464 Cedano Prieto DM ; Cheng Y ; Chang CC ; Yu J ; Takada YK ; Takada Y PLoS One 2017[]; 12 (9 ): e0184285 PMID28873464 show ga We have reported that integrins crosstalk with growth factors through direct binding to growth factors (e.g., fibroblast growth factor-1, insulin-like growth factor 1 (IGF1), neuregulin-1, fractalkine) and subsequent ternary complex formation with cognate receptor [e.g., integrin/IGF1/IGF1 receptor (IGF1R)]. IGF1 and IGF2 are overexpressed in cancer and major therapeutic targets. We previously reported that IGF1 binds to integrins ???3 and ?6?4, and the R36E/R37E mutant in the C-domain of IGF1 is defective integrin binding and signaling functions of IGF1, and acts as an antagonist of IGF1R. We studied if integrins play a role in the signaling functions of IGF2, another member of the IGF family. Here we describe that IGF2 specifically binds to integrins ???3 and ?6?4, and induced proliferation of CHO cells (IGF1R+) that express ???3 or ?6?4 (?3- or ?6?4-CHO cells). Arg residues to Glu at positions 24, 34, 37 and/or 38 in or close to the C-domain of IGF2 play a critical role in binding to integrins and signaling functions. The R24E/R37E/R38E, R34E/R37E/R38E, and R24E/R34E/R37E/R38E mutants were defective in integrin binding and IGF2 signaling. These mutants suppressed proliferation induced by WT IGF2, suggesting that they are dominant-negative antagonists of IGF1R. These results suggest that IGF2 also requires integrin binding for signaling functions, and the IGF2 mutants that cannot bind to integrins act as antagonists of IGF1R. The present study defines the role of the C-domain in integrin binding and signaling. |*Signal Transduction [MESH] |Amino Acid Sequence [MESH] |Animals [MESH] |CHO Cells [MESH] |Cell Line, Tumor [MESH] |Cell Proliferation [MESH] |Cricetinae [MESH] |Cricetulus [MESH] |Humans [MESH] |Insulin-Like Growth Factor II/*chemistry/*metabolism [MESH] |Integrin alpha6beta4/*metabolism [MESH] |Integrin alphaVbeta3/*metabolism [MESH] |Mutant Proteins [MESH] |Protein Binding [MESH] |Protein Domains [MESH] |Receptor, IGF Type 1/*metabolism [MESH]Direct integrin binding to insulin-like growth factor-2 through the C-(epmc).pdf DeepDyve Pubget Overpricing