Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

The type iii effector espf coordinates membrane trafficking by the spatiotemporal activation of two eukaryotic signaling pathways

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Alto, N. M.
  • Weflen, A. W.
  • Rardin, M. J.
  • Yarar, D.
  • Lazar, C. S.
  • Tonikian, R.
  • Koller, A.
  • Taylor, S. S.
  • Boone, C.
  • Sidhu, S. S.
  • Schmid, Sandra
  • Hecht, G. A.
  • Dixon, J. E.

publication date

  • September 2007

journal

  • Journal of Cell Biology  Journal

abstract

  • Bacterial toxins and effector proteins hijack eukaryotic enzymes that are spatially localized and display rapid signaling kinetics. However, the molecular mechanisms by which virulence factors engage highly dynamic substrates in the host cell environment are poorly understood. Here, we demonstrate that the enteropathogenic Escherichia coli (EPEC) type III effector protein EspF nucleates a multiprotein signaling complex composed of eukaryotic sorting nexin 9 (SNX9) and neuronal Wiskott-Aldrich syndrome protein (N-WASP). We demonstrate that a specific and high affinity association between EspF and SNX9 induces membrane remodeling in host cells. These membrane-remodeling events are directly coupled to N-WASP/Arp2/3-mediated actin nucleation. In addition to providing a biochemical mechanism of EspF function, we find that EspF dynamically localizes to membrane-trafficking organelles in a spatiotemporal pattern that correlates with SNX9 and N-WASP activity in living cells. Thus, our findings suggest that the EspF-dependent assembly of SNX9 and N-WASP represents a novel form of signaling mimicry used to promote EPEC pathogenesis and gastrointestinal disease.

subject areas

  • Actin-Related Protein 2-3 Complex
  • Actins
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins
  • Cell Membrane
  • Cell Polarity
  • Cell Survival
  • Dogs
  • Epithelial Cells
  • Escherichia coli
  • Escherichia coli Proteins
  • Eukaryotic Cells
  • Evolution, Molecular
  • HeLa Cells
  • Humans
  • Ligands
  • Mice
  • Molecular Sequence Data
  • Protein Binding
  • Protein Transport
  • Signal Transduction
  • Vesicular Transport Proteins
  • Wiskott-Aldrich Syndrome Protein, Neuronal
  • src Homology Domains
scroll to property group menus

Identity

PubMed Central ID

  • PMC2064658

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200705021

PubMed ID

  • 17893247
scroll to property group menus

Additional Document Info

start page

  • 1265

end page

  • 1278

volume

  • 178

issue

  • 7

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support