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10.1091/mbc.E14-10-1463 http://scihub22266oqcxt.onion/10.1091/mbc.E14-10-1463 C4325837!4325837 !25540428     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25540428 &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 2015 ; 26 (4 ): 659-73 Nephropedia Template TP {{tp|p=25540428 |t=2015. ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1) |pdf=|usr=}}{{25540428 }} gab.com Text ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1) JO: Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25540428 #FOAvip Discoidin domain receptor 1 (DDR1) is a receptor tyrosine kinase that binds and transmits signals from various collagens in epithelial cells. However, how DDR1-dependent signaling is regulated has not been understood. Here we report that collagen binding induces ADAM10-dependent ectodomain shedding of DDR1. DDR1 shedding is not a result of an activation of its signaling pathway, since DDR1 mutants defective in signaling were shed in an efficient manner. DDR1 and ADAM10 were found to be in a complex on the cell surface, but shedding did not occur unless collagen bound to DDR1. Using a shedding-resistant DDR1 mutant, we found that ADAM10-dependent DDR1 shedding regulates the half-life of collagen-induced phosphorylation of the receptor. Our data also revealed that ADAM10 plays an important role in regulating DDR1-mediated cell adhesion to achieve efficient cell migration on collagen matrices. Twit Text FOAVip ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1) ????Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25540428 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25540428 #FOAvip English Wikipedia <ref>{{Cite pmid|25540428 }}</ref> ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1) #MMPMID25540428 Shitomi Y ; Thøgersen IB ; Ito N ; Leitinger B ; Enghild JJ ; Itoh Y Mol Biol Cell 2015[Feb]; 26 (4 ): 659-73 PMID25540428 show ga Discoidin domain receptor 1 (DDR1) is a receptor tyrosine kinase that binds and transmits signals from various collagens in epithelial cells. However, how DDR1-dependent signaling is regulated has not been understood. Here we report that collagen binding induces ADAM10-dependent ectodomain shedding of DDR1. DDR1 shedding is not a result of an activation of its signaling pathway, since DDR1 mutants defective in signaling were shed in an efficient manner. DDR1 and ADAM10 were found to be in a complex on the cell surface, but shedding did not occur unless collagen bound to DDR1. Using a shedding-resistant DDR1 mutant, we found that ADAM10-dependent DDR1 shedding regulates the half-life of collagen-induced phosphorylation of the receptor. Our data also revealed that ADAM10 plays an important role in regulating DDR1-mediated cell adhesion to achieve efficient cell migration on collagen matrices. |*Cell Movement [MESH] |*Signal Transduction [MESH] |ADAM Proteins/genetics/metabolism/*physiology [MESH] |ADAM10 Protein [MESH] |Amino Acid Sequence [MESH] |Amyloid Precursor Protein Secretases/genetics/metabolism/*physiology [MESH] |Cell Adhesion [MESH] |Collagen/*metabolism [MESH] |Discoidin Domain Receptor 1 [MESH] |Gene Knockdown Techniques [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Membrane Proteins/genetics/metabolism/*physiology [MESH] |Molecular Sequence Data [MESH] |Protein Structure, Tertiary [MESH]ADAM10 controls collagen signaling and cell migration on collagen by s(epmc).pdf DeepDyve Pubget Overpricing