ABM-1 and ABM-2 homology sequences: consensus docking sites for actin-based motility defined by oligoproline regions in Listeria ActA surface protein and human VASP

Biochem Biophys Res Commun. 1997 Feb 24;231(3):686-91. doi: 10.1006/bbrc.1997.6158.

Abstract

Actin-based motility involves a cascade of binding interactions designed to assemble actin regulatory proteins into functional locomotory units. Listeria ActA surface protein contains a series of nearly identical EFPPPPTDE-type oligoproline sequences for binding vasodilator-stimulated phosphoprotein (VASP). The latter is a tetrameric protein with numerous GPP-PPP docking sites for profilin, a 15 kDa regulatory protein that promotes actin filament assembly. Analysis of known actin regulatory proteins led to the identification of distinct Actin-Based Motility homology sequences ABM-1; (D/E)FPPPPX(D/E); and ABM-2, XPPPPP (where X denotes G, A, L, and S).

MeSH terms

  • Actins / chemistry*
  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry*
  • Binding Sites
  • Cell Adhesion Molecules / chemistry*
  • Consensus Sequence
  • Contractile Proteins*
  • Humans
  • Membrane Proteins / chemistry*
  • Microfilament Proteins / chemistry*
  • Molecular Sequence Data
  • Phosphoproteins / chemistry*
  • Profilins
  • Proline / chemistry
  • Protein Binding

Substances

  • Actins
  • Bacterial Proteins
  • Cell Adhesion Molecules
  • Contractile Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • Phosphoproteins
  • Profilins
  • vasodilator-stimulated phosphoprotein
  • actA protein, Listeria monocytogenes
  • Proline