Adhesion‐dependent Caveolin‐1 Tyrosine‐14 phosphorylation is regulated by FAK in response to changing matrix stiffness
نویسندگان
چکیده
Integrin-mediated adhesion regulates cellular responses to changes in the mechanical and biochemical properties of extracellular matrix. Cell–matrix caveolar endocytosis, dependent on caveolin 1 (Cav1) Tyr14 phosphorylation (pY14Cav1), control anchorage-dependent signaling. We find that cell–matrix pY14Cav1 levels mouse fibroblasts. Biochemical fractionation reveals endogenous be present caveolae focal adhesions (FA). Adhesion does not affect pY14Cav1, supporting its regulation at FA, which PF-228-mediated inhibition kinase (FAK) disrupts. Cell 2D polyacrylamide matrices increasing stiffness stimulates Cav1 phosphorylation, is comparable FAK. Inhibition FAK across varying stiffnesses shows it more prominently higher stiffness. Taken together, these studies reveal presence FAK–pY14Cav1 crosstalk regulated by adhesion.
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2021
ISSN: ['0014-5793', '1873-3468']
DOI: https://doi.org/10.1002/1873-3468.14025