Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 24 April 2001
Vol. 2001, Issue 79, p. tw3
[DOI: 10.1126/stke.2001.79.tw3]


Cell Biology Linking Actin to Endocytosis

Although the actin cytoskeleton has been implicated in endocytosis, the molecular basis for its involvement has not been clear. Kessels et al. report that mammalian actin-binding protein 1 (mAbp1) associates with dynamin, a guanosine triphosphatase (GTPase) that is essential in forming clathrin-coated vesicles during receptor-mediated endocytosis. Dynamin and mAbp1 from rat brain extract could be isolated in a complex, and the SH3 domain of mAbp1 was required for the interaction in transfected cells. MAbp1 colocalized with actin and dynamin at sites involved in synapse formation in cortical regions of the hippocampus. Its localization to dynamin-rich sites of endocytosis in fibroblasts was dependent on growth receptor activation. Because Abp1 proteins in different species interact with various kinases including Src, the authors propose that mAbp1 may act as an adaptor protein that links signals from membrane receptors to the actin cytoskeleton and to the endocytic machinery.

M. M. Kessels, A. E. Y. Engqvist-Goldstein, D. G. Drubin, B. Qualmann, Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dyanmin. J. Cell Biol. 153, 351-366 (2001). [Abstract] [Full Text]

Citation: Linking Actin to Endocytosis. Sci. STKE 2001, tw3 (2001).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882