Molecular analysis of the interaction between palladin and alpha-actinin

FEBS Lett. 2004 May 21;566(1-3):30-4. doi: 10.1016/j.febslet.2004.04.006.

Abstract

Palladin is a novel component of stress fiber dense regions. Antisense and transient overexpression studies have indicated an important role for palladin in the regulation of actin cytoskeleton. Palladin colocalizes and coimmunoprecipitates with alpha-actinin, a dense region component, but the molecular details and functional significance of the interaction have not been studied. We show here a direct association between the two proteins and have mapped the binding site within a short sequence of palladin and in the carboxy-terminal calmodulin domain of alpha-actinin. Using transfection-based targeting assays, we show that palladin is involved in targeting of alpha-actinin to specific subcellular foci indicating a functional interplay between the two actin-associated proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actinin / genetics
  • Actinin / metabolism*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CHO Cells
  • COS Cells
  • Cell Line, Tumor
  • Chemical Precipitation
  • Chlorocebus aethiops
  • Cricetinae
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Humans
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Protein Interaction Mapping / methods
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / genetics
  • Sequence Alignment
  • Transfection
  • Two-Hybrid System Techniques

Substances

  • Cytoskeletal Proteins
  • PALLD protein, human
  • Phosphoproteins
  • Recombinant Proteins
  • Actinin