CrkL directs ASAP1 to peripheral focal adhesions

Oda, A. et al. (2003) CrkL directs ASAP1 to peripheral focal adhesions. Journal of Biological Chemistry, 278(8), pp. 6456-6460. (doi: 10.1074/jbc.M210817200) (PMID:12522101)

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Searching for proteins in platelets that can interact with the N-terminal SH3 domain of CrkL (using a combination of a pull-down assay followed by mass spectrometry), we have found that human platelets express an ADP-ribosylation factor (Arf)-specific GTPase-activating protein (GAP), ASAP1, as a CrkL-binding protein. In spreading platelets, most endogenous ASAP1 is localized at peripheral focal adhesions. To determine the physiologic significance of the CrkL-ASAP1 association, we overexpressed CrkL, ASAP1, or both in combination in COS7 cells. Unlike endogenous ASAP1 in platelets, overexpressed ASAP1 showed diffuse cytoplasmic distribution. However, when co-expressed with wild-type CrkL, both endogenous and expressed ASAP1 accumulated at CrkL-induced focal adhesions. An SH2-mutated CrkL, which cannot localize at focal adhesions, failed to recruit ASAP1 into focal adhesions. Thus, CrkL appears to be a lynchpin between ASAP1 and peripheral focal adhesions.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Machesky, Professor Laura
Authors: Oda, A., Wada, I., Miura, K., Okawa, K., Kadoya, T., Kato, T., Nishihara, H., Maeda, M., Tanaka, S., Nagashima, K., Nishitani, C., Matsuno, K., Ishino, M., Machesky, L. M., Fujita, H., and Randazzo, P.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cancer Sciences
Journal Name:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology
ISSN (Online):1083-351X
Published Online:08 January 2003
Copyright Holders:Copyright © 2003 ASBMB
First Published:First published in Journal of Biological Chemistry 278(8): 6456-6460
Publisher Policy:Reproduced under a Creative Commons License

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