2004
DOI: 10.1002/cm.10173
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Palladin is a novel binding partner for Ena/VASP family members

Abstract: 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. The… Show more

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Cited by 77 publications
(87 citation statements)
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References 65 publications
(102 reference statements)
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“…This distinctive molecular function is likely to underlie the dramatic effects on actin organization that result from palladin overexpression (16,23). It is interesting to note that palladin binds to three other proteins that have been shown to cross-link actin filaments in vitro: ␣-actinin, VASP, and Eps8 (22)(23)(24). This observation raises some interesting questions about the evolution of actin-bundling proteins in vertebrate cells: do these multiple actin cross-linking proteins function synergistically or redundantly, or do they possess subtle functional differences in their ability to generate multifilament arrays?…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…This distinctive molecular function is likely to underlie the dramatic effects on actin organization that result from palladin overexpression (16,23). It is interesting to note that palladin binds to three other proteins that have been shown to cross-link actin filaments in vitro: ␣-actinin, VASP, and Eps8 (22)(23)(24). This observation raises some interesting questions about the evolution of actin-bundling proteins in vertebrate cells: do these multiple actin cross-linking proteins function synergistically or redundantly, or do they possess subtle functional differences in their ability to generate multifilament arrays?…”
Section: Discussionmentioning
confidence: 99%
“…Within smooth muscle and non-muscle cells, palladin localizes to actin filaments in regularly spaced puncta that have also been found to contain ␣-actinin (23) and vasodilator-stimulated phosphoprotein (VASP) 4 (24). Palladin possesses a large number of molecular partners, including a cohort of proteins that bind directly to actin: ␣-actinin (23), VASP (24), profilin (25), ezrin (17), and Eps8 (22). Palladin also binds to a second cohort of proteins that indirectly influence actin organization: ArgBP2 (26), LPP (27), and SPIN90 (28).…”
mentioning
confidence: 99%
“…Analysis of the palladin sequence revealed a number of consensus motifs that function as binding sites for known actin-regulating proteins. The N-terminal half of palladin contains polyproline stretches that bind to members of the Ena/Mena/VASP family of proteins (Boukhelifa et al, 2004). Within its N-terminal half, palladin also contains a binding site for the filament crosslinking protein, ␣-actinin (Ronty et al, 2004).…”
Section: Introductionmentioning
confidence: 99%
“…Palladin is a multi-domain, actin-binding protein which binds directly to F-actin and many other actin-binding proteins, including profilin, VASP, ezrin, Lasp-1, EPS8, CLP-36, α-actinin and ArgBP2 [30][31][32][33][34][35][36][37]. Palladin is a cytoskeletal protein that controls stress fiber integrity, and is expressed in epithelial and mesenchymal cells [38,39].…”
Section: Discussionmentioning
confidence: 99%