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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.<\/jats:p>","DOI":"10.1091\/mbc.e14-10-1463","type":"journal-article","created":{"date-parts":[[2014,12,25]],"date-time":"2014-12-25T03:32:38Z","timestamp":1419478358000},"page":"659-673","source":"Crossref","is-referenced-by-count":56,"title":["ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1)"],"prefix":"10.1091","volume":"26","author":[{"given":"Yasuyuki","family":"Shitomi","sequence":"first","affiliation":[{"name":"Kennedy Institute of Rheumatology, Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, University of Oxford, Oxford OX3 7FY, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ida B.","family":"Th\u00f8gersen","sequence":"additional","affiliation":[{"name":"Department of Molecular 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