期刊
CELL MOTILITY AND THE CYTOSKELETON
卷 58, 期 1, 页码 17-29出版社
WILEY-LISS
DOI: 10.1002/cm.10173
关键词
actin; stress fibers; focal adhesion; zyxin; vinculin; cell spreading
类别
资金
- NIGMS NIH HHS [GM61743] Funding Source: Medline
- NINDS NIH HHS [NS43243] Funding Source: Medline
Palladin is an actin-associated protein that contains proline-rich motifs within its amino-terminal sequence that are similar to motifs found in zyxin, vinculin, and the Listeria protein ActA. These motifs are known to be potential binding sites for the Vasodilator-Stimulated Phosphoprotein (VASP). Here, we demonstrate that palladin is an additional direct binding partner for VASP, by using co-immunoprecipitation and blot overlay techniques with both endogenous palladin and recombinant myc-tagged palladin. These results show that VASP binds to full-length palladin and also to the amino-terminal half of palladin, where the polyproline motifs are located. Using a synthetic peptide array, two discrete binding sites for VASP were identified within palladin's proline-rich amino-terminal domain. Using double-label immunofluorescence staining of fully-spread and actively-spreading fibroblasts, the extent of co-localization of palladin and VASP was explored. These proteins were found to strongly co-localize along stress fibers, and partially co-localize in focal adhesions, lamellipodia, and focal complexes. These results suggest that the recently described actin-associated protein palladin may play an important role in recruiting VASP to sites of actin filament growth, anchorage, and crosslinking. Cell Motil. Cytoskeleton 58:17-29, 2004. (C) 2004 Wiley-Liss, Inc.
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