Abstract
Focal adhesion kinase (pp125FAK) is localized to focal adhesions and tyrosine phosphorylated by the engagement of beta 1 integrins. However, it is unclear how pp125FAK is linked to integrin molecules. We demonstrate that pp125FAK is directly associated with paxillin, a 68-kD cytoskeleton protein. The COOH-terminal domain of pp125FAK spanning FAK residues 919-1042 is sufficient for paxillin binding and has vinculin-homologous amino acids, which are essential for paxillin binding. Microinjection and subsequent immunohistochemical analysis reveal that glutathione S-transferase-FAK fusion proteins, which bind to paxillin, localize to focal adhesions, whereas fusion proteins with no paxillin-binding activity do not localize to focal adhesions. These findings strongly suggest that pp125FAK is localized to focal adhesions by the direct association with paxillin.
Dates
Type | When |
---|---|
Created | 21 years, 2 months ago (June 24, 2004, 3:56 a.m.) |
Deposited | 2 years, 1 month ago (July 25, 2023, 2:56 a.m.) |
Indexed | 3 months, 1 week ago (May 19, 2025, 8:30 a.m.) |
Issued | 29 years, 10 months ago (Oct. 1, 1995) |
Published | 29 years, 10 months ago (Oct. 1, 1995) |
Published Online | 29 years, 10 months ago (Oct. 1, 1995) |
Published Print | 29 years, 10 months ago (Oct. 1, 1995) |
@article{Tachibana_1995, title={Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK.}, volume={182}, ISSN={1540-9538}, url={http://dx.doi.org/10.1084/jem.182.4.1089}, DOI={10.1084/jem.182.4.1089}, number={4}, journal={The Journal of experimental medicine}, publisher={Rockefeller University Press}, author={Tachibana, K and Sato, T and D’Avirro, N and Morimoto, C}, year={1995}, month=oct, pages={1089–1099} }