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Vol. 11, Issue 1, 393-412, January 2000
Department of Molecular and Cell Biology, University of California,
Berkeley, Berkeley, California 94720-3202
Yeast Abp1p is a cortical actin cytoskeleton protein implicated in
cytoskeletal regulation, endocytosis, and cAMP-signaling. We have
identified a gene encoding a mouse homologue of Abp1p, and it is
identical to SH3P7, a protein shown recently to be a target of Src
tyrosine kinases. Yeast and mouse Abp1p display the same domain
structure including an N-terminal actin-depolymerizing factor homology
domain and a C-terminal Src homology 3 domain. Using two independent
actin-binding domains, mAbp1 binds to actin filaments with a 1:5
saturation stoichiometry. In stationary cells, mAbp1 colocalizes with
cortical F-actin in fibroblast protrusions that represent sites of
cellular growth. mAbp1 appears at the actin-rich leading edge of
migrating cells. Growth factors cause mAbp1 to rapidly accumulate in
lamellipodia. This response can be mimicked by expression of
dominant-positive Rac1. mAbp1 recruitment appears to be dependent on de
novo actin polymerization and occurs specifically at sites enriched for
the Arp2/3 complex. mAbp1 is a newly identified cytoskeletal protein in
mice and may serve as a signal-responsive link between the dynamic
cortical actin cytoskeleton and regions of membrane dynamics.
Corresponding author. E-mail address:
drubin{at}uclink4.berkeley.edu.
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