PMID- 14983521
OWN - NLM
STAT- MEDLINE
DCOM- 20041109
LR  - 20210108
IS  - 0886-1544 (Print)
IS  - 0886-1544 (Linking)
VI  - 58
IP  - 1
DP  - 2004 May
TI  - Palladin is a novel binding partner for Ena/VASP family members.
PG  - 17-29
AB  - 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.
CI  - Copyright 2004 Wiley-Liss, Inc.
FAU - Boukhelifa, Malika
AU  - Boukhelifa M
AD  - Department of Cell and Molecular Physiology, University of North Carolina at 
      Chapel Hill, 27599-7545, USA.
FAU - Parast, Mana M
AU  - Parast MM
FAU - Bear, James E
AU  - Bear JE
FAU - Gertler, Frank B
AU  - Gertler FB
FAU - Otey, Carol A
AU  - Otey CA
LA  - eng
GR  - GM61743/GM/NIGMS NIH HHS/United States
GR  - NS43243/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell Motil Cytoskeleton
JT  - Cell motility and the cytoskeleton
JID - 8605339
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (ENA-VASP proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Metalloproteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (PALLD protein, human)
RN  - 0 (Phosphoproteins)
RN  - 0 (ZYX protein, human)
RN  - 0 (Zyx protein, mouse)
RN  - 0 (Zyxin)
RN  - 0 (palladin protein, mouse)
RN  - 0 (vasodilator-stimulated phosphoprotein)
RN  - 125361-02-6 (Vinculin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Adhesion Molecules/genetics/*metabolism
MH  - Cells, Cultured
MH  - Chick Embryo
MH  - Cytoskeletal Proteins/genetics/*metabolism
MH  - DNA-Binding Proteins/genetics/*metabolism
MH  - Fibroblasts/metabolism
MH  - Glycoproteins
MH  - Humans
MH  - Metalloproteins/genetics/metabolism
MH  - Mice
MH  - Microfilament Proteins
MH  - Molecular Sequence Data
MH  - Phosphoproteins/genetics/*metabolism
MH  - Protein Binding
MH  - Sequence Homology, Amino Acid
MH  - Vinculin/genetics/metabolism
MH  - Zyxin
EDAT- 2004/02/26 05:00
MHDA- 2004/11/13 09:00
CRDT- 2004/02/26 05:00
PHST- 2004/02/26 05:00 [pubmed]
PHST- 2004/11/13 09:00 [medline]
PHST- 2004/02/26 05:00 [entrez]
AID - 10.1002/cm.10173 [doi]
PST - ppublish
SO  - Cell Motil Cytoskeleton. 2004 May;58(1):17-29. doi: 10.1002/cm.10173.