期刊
MOLECULAR BIOLOGY OF THE CELL
卷 26, 期 4, 页码 659-673出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E14-10-1463
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资金
- Arthritis Research UK core grant
- Arthritis Research UK Programme Grant [19797]
- Cancer Research UK Project Grant [C1507/A12015]
- MRC [G0802007] Funding Source: UKRI
- Medical Research Council [G0802007] Funding Source: researchfish
- Versus Arthritis [19797] Funding Source: researchfish
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.
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