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

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 protei...

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Bibliographic Details
Published in:Molecular medicine (Cambridge, Mass.) Mass.), 1998-10, Vol.4 (10), p.675-687
Main Authors: Schreiber, V, Moog-Lutz, C, Régnier, C H, Chenard, M P, Boeuf, H, Vonesch, J L, Tomasetto, C, Rio, M C
Format: Article
Language:English
Subjects:
3T3 Cells
Actins - metabolism
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Animals
Binding Sites
Biochemistry, Molecular Biology
Breast Neoplasms - metabolism
Breast Neoplasms - pathology
Cancer
Cell Membrane - metabolism
Cell Transformation, Neoplastic
COS Cells
Cytoskeletal Proteins
Female
Homeodomain Proteins - genetics
Homeodomain Proteins - metabolism
Humans
Life Sciences
LIM Domain Proteins
Mice
Microfilament Proteins - genetics
Microfilament Proteins - metabolism
Molecular Sequence Data
Neoplasm Proteins
Phosphorylation
Proto-Oncogene Proteins pp60(c-src) - genetics
src Homology Domains - genetics
Subcellular Fractions
Tumor Cells, Cultured
Tyrosine - metabolism
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Summary: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.
ISSN:1076-1551
1528-3658
DOI:10.1007/bf03401929