RRC ID 3142
Author Hanajima-Ozawa M, Matsuzawa T, Fukui A, Kamitani S, Ohnishi H, Abe A, Horiguchi Y, Miyake M.
Title Enteropathogenic Escherichia coli, Shigella flexneri, and Listeria monocytogenes recruit a junctional protein, zonula occludens-1, to actin tails and pedestals.
Journal Infect Immun
Abstract Enteropathogenic Escherichia coli, Shigella flexneri, and Listeria monocytogenes induce localized actin polymerization at the cytoplasmic face of the plasma membrane or within the host cytoplasm, creating unique actin-rich structures termed pedestals or actin tails. The process is known to be mediated by the actin-related protein 2 and 3 (Arp2/3) complex, which in these cases acts downstream of neural Wiskott-Aldrich syndrome protein (N-WASP) or of a listerial functional homolog of WASP family proteins. Here, we show that zonula occludens-1 (ZO-1), a protein in the tight junctions of polarized epithelial cells, is recruited to actin tails and pedestals. Immunocytochemical analysis revealed that ZO-1 was stained most in the distal part of the actin-rich structures, and the incorporation was mediated by the proline-rich region of the ZO-1 molecule. The direct clustering of membrane-targeted Nck, which is known to activate the N-WASP-Arp2/3 pathway, triggered the formation of the ZO-1-associated actin tails. The results suggest that the activation of the Arp2/3 complex downstream of N-WASP or a WASP-related molecule is a key to the formation of the particular actin-rich structures that bind with ZO-1. We propose that an analysis of the recruitment on a molecular basis will lead to an understanding of how ZO-1 recognizes a distinctive actin-rich structure under pathophysiological conditions.
Volume 75(2)
Pages 565-73
Published 2007-2-1
DOI 10.1128/IAI.01479-06
PII IAI.01479-06
PMID 17118974
PMC PMC1828484
MeSH Actin-Related Protein 2 / metabolism Actin-Related Protein 3 / metabolism Actins / metabolism* Adaptor Proteins, Signal Transducing Animals Cytoplasm / chemistry Epithelial Cells / microbiology* Escherichia coli / physiology* HeLa Cells Humans Immunohistochemistry Listeria monocytogenes / physiology* Membrane Proteins / metabolism* Mice Microscopy, Fluorescence NIH 3T3 Cells Oncogene Proteins / physiology Phosphoproteins / metabolism* Shigella flexneri / physiology* Zonula Occludens-1 Protein
IF 3.201
Times Cited 26
Pathogenic microorganisms L. monocytogenes(RIMD 1205001) S. flexneri 2a?