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PMID: 12134077 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Contribution of Ena/VASP proteins to intracellular motility of listeria requires phosphorylation and proline-rich core but not F-actin binding or multimerization.

Molecular biology of the cell ·Vol. 13 ·No. 7 ·2002-07-00 ·Pages 2383-96

Geese M, Loureiro JJ, Bear JE, Wehland J, Gertler FB, Sechi AS

Abstract

The Listeria model system has been essential for the identification and characterization of key regulators of the actin cytoskeleton such as the Arp2/3 complex and Ena/vasodilator-stimulated phosphoprotein (VASP) proteins. Although the role of Ena/VASP proteins in Listeria motility has been extensively studied, little is known about the contributions of their domains and phosphorylation state to bacterial motility. To address these issues, we have generated a panel of Ena/VASP mutants and, upon expression in Ena/VASP-deficient cells, evaluated their contribution to Ena/VASP function in Listeria motility. The proline-rich region, the putative G-actin binding site, and the Ser/Thr phosphorylation of Ena/VASP proteins are all required for efficient Listeria motility. Surprisingly, the interaction of Ena/VASP proteins with F-actin and their potential ability to form multimers are both dispensable for their involvement in this process. Our data suggest that Ena/VASP proteins contribute to Listeria motility by regulating both the nucleation and elongation of actin filaments at the bacterial surface.

MeSH Terms
Actins/metabolism Animals Binding Sites Carrier Proteins/genetics,metabolism Cell Adhesion Molecules/chemistry,genetics,metabolism Cell Line Cell Movement/physiology Contractile Proteins Cytoskeletal Proteins Fibroblasts/cytology,metabolism Listeria/metabolism Luminescent Proteins/metabolism Microfilament Proteins/genetics,metabolism Mutagenesis, Site-Directed Phosphoproteins/chemistry,genetics,metabolism Phosphorylation Polymers/metabolism Profilins Proline/metabolism Protein Binding Protein Structure, Tertiary Recombinant Fusion Proteins/genetics,metabolism Thymosin/genetics,metabolism
Chemicals
Actins Carrier Proteins Cell Adhesion Molecules Contractile Proteins Cytoskeletal Proteins Enah protein, mouse Luminescent Proteins Microfilament Proteins Phosphoproteins Polymers Profilins Recombinant Fusion Proteins vasodilator-stimulated phosphoprotein thymosin beta(4) Thymosin Proline
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Geese Marcus
Department of Cell Biology, Gesellschaft für Biotechnologische Forschung, D-38124 Braunschweig, Germany.
Loureiro Joseph J
Bear James E
Wehland Jürgen
Gertler Frank B
Sechi Antonio S
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
DOI
10.1091/mbc.e02-01-0058
Published
2002-07-00
Pages
2383-96
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC117321
Subset
IM
Grants
NIGMS NIH HHS · R01 GM058801 · United States
NIGMS NIH HHS · GM-58801 · United States
External Links
PubMed source DOI: 10.1091/mbc.e02-01-0058 PMC Full Text View journal details
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