期刊
NATURE CELL BIOLOGY
卷 15, 期 6, 页码 625-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb2747
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资金
- ERC
- DFG
- Max Planck Society
How different integrins that bind to the same type of extracellular matrix protein mediate specific functions is unclear. We report the functional analysis of beta(1)- and alpha(v)-class integrins expressed in pan-integrin-null fibroblasts seeded on fibronectin. Reconstitution with beta(1)-class integrins promotes myosin-II-independent formation of small peripheral adhesions and cell protrusions, whereas expression of alpha(v)-class integrins induces the formation of large focal adhesions. Co-expression of both integrin classes leads to full myosin activation and traction-force development on stiff fibronectin-coated substrates, with alpha(v)-class integrins accumulating in adhesion areas exposed to high traction forces. Quantitative proteomics linked alpha v-class integrins to a GEF-H1-RhoA pathway coupled to the formin mDia1 but not myosin II, and alpha(5)beta(1) integrins to a RhoA-Rock-myosin II pathway. Our study assigns specific functions to distinct fibronectin-binding integrins, demonstrating that alpha(5)beta(1) integrins accomplish force generation, whereas alpha(v)-class integrins mediate the structural adaptations to forces, which cooperatively enable cells to sense the rigidity of fibronectin-based microenvironments.
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