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. 1998 Oct;4(10):675–687.

Lasp-1, a novel type of actin-binding protein accumulating in cell membrane extensions.

V Schreiber 1, C Moog-Lutz 1, C H Régnier 1, M P Chenard 1, H Boeuf 1, J L Vonesch 1, C Tomasetto 1, M C Rio 1
PMCID: PMC2230251  PMID: 9848085

Abstract

The Lasp-1 gene, which has been localized to the q12-q21 region of human chromosome 17, is amplified and overexpressed in human breast cancers. In addition to the previously reported LIM and SH3 domains of Lasp-1, we report here the identification of an actin-binding domain in the core of the protein. This domain is functional as we demonstrate that Lasp-1 binds actin in vivo and in vitro. In addition, confocal analysis of the Lasp-1 subcellular distribution shows that the protein is colocalized with actin at peripheral cell extensions in individual epithelial cancer cells and in transformed fibroblastic cells. Moreover, Lasp-1 is tyrosine phosphorylated in fibroblast cell lines transformed by a constitutively active form of c-Src (c-SrcY527F). Altogether, our results show that Lasp-1 defines a new type of actin-binding protein and suggest that the protein may play a role in a signaling pathway involved in the organization of the cytoskeleton.

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