Identification of a cofilin-like actin-binding site on translationally controlled tumor protein (TCTP)

FEBS Lett. 2010 Dec 1;584(23):4756-60. doi: 10.1016/j.febslet.2010.10.054. Epub 2010 Oct 29.

Abstract

Translationally controlled tumor protein (TCTP) expression is suppressed during cancer cell reversion to a non-malignant phenotype. We identified a primary sequence of TCTP with homology to ADF/cofilin. We confirm that a synthetic peptide corresponding to this sequence binds specifically to actin and is displaced from actin by cofilin. TCTP peptide has higher affinity for G-actin than F-actin and does not block actin-filament depolymerization by cofilin. These results suggest that TCTP may channel active cofilin to F-actin, enhancing the cofilin-activity cycle in invasive tumor cells. Loss of TCTP may result in sequestration of active cofilin by a monomeric pool of actin.

Publication types

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

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Actin Depolymerizing Factors / metabolism*
  • Actins / chemistry
  • Actins / metabolism*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Biomarkers, Tumor / chemistry*
  • Biomarkers, Tumor / metabolism*
  • Humans
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Rabbits
  • Rats
  • Substrate Specificity
  • Tumor Protein, Translationally-Controlled 1

Substances

  • Actin Depolymerizing Factors
  • Actins
  • Biomarkers, Tumor
  • Peptide Fragments
  • TPT1 protein, human
  • Tpt1 protein, mouse
  • Tpt1 protein, rat
  • Tumor Protein, Translationally-Controlled 1