Exploiting pathogenic Escherichia coli to model transmembrane receptor signalling

被引:72
作者
Hayward, RD
Leong, JM
Koronakis, V
Campellone, KG
机构
[1] Univ Massachusetts, Sch Med, Dept Mol Genet & Microbiol, Worcester, MA 01655 USA
[2] Univ Cambridge, Dept Pathol, Cambridge CB2 1QP, England
基金
英国医学研究理事会; 英国惠康基金;
关键词
D O I
10.1038/nrmicro1391
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Many microbial pathogens manipulate the actin cytoskeleton of eukaryotic target cells to promote their internalization, intracellular motility and dissemination. Enteropathogenic and enterohaemorrhagic Escherichia coli, which both cause severe diarrhoeal disease, can adhere to mammalian intestinal cells and induce reorganization of the actin cytoskeleton into 'pedestal-like' pseudopods beneath the extracellular bacteria. As pedestal assembly is triggered by E. coli virulence factors that mimic several host cell-signalling components, such as transmembrane receptors, their cognate ligands and cytoplasmic adaptor proteins, it can serve as a powerful model system to study eukaryotic transmembrane signalling. Here, we consider the impact of recent data on our understanding of both E. coli pathogenesis and cell biology, and the rich prospects for exploiting these bacterial factors as versatile tools to probe cellular signalling pathways.
引用
收藏
页码:358 / 370
页数:13
相关论文
共 127 条
[1]   Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein [J].
Abdul-Manan, N ;
Aghazadeh, B ;
Liu, GA ;
Majumdar, A ;
Ouerfelli, O ;
Siminovitch, KA ;
Rosen, MK .
NATURE, 1999, 399 (6734) :379-383
[2]   Identification of a bacterial type III effector family with G protein mimicry functions [J].
Alto, NM ;
Shao, F ;
Lazar, CS ;
Brost, RL ;
Chua, G ;
Mattoo, S ;
McMahon, SA ;
Ghosh, P ;
Hughes, TR ;
Boone, C ;
Dixon, JE .
CELL, 2006, 124 (01) :133-145
[3]   The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck [J].
Anton, IM ;
Lu, WG ;
Mayer, BJ ;
Ramesh, N ;
Geha, RS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (33) :20992-20995
[4]   Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli [J].
Batchelor, M ;
Prasannan, S ;
Daniell, S ;
Reece, S ;
Connerton, I ;
Bloomberg, G ;
Dougan, G ;
Frankel, G ;
Matthews, S .
EMBO JOURNAL, 2000, 19 (11) :2452-2464
[5]   Agents that inhibit Rho, Rac, and Cdc42 do not block formation of actin pedestals in HeLa cells infected with enteropathogenic Escherichia coli [J].
Ben-Ami, G ;
Ozeri, V ;
Hanski, E ;
Hofmann, F ;
Aktories, K ;
Hahn, KM ;
Bokoch, GM ;
Rosenshine, I .
INFECTION AND IMMUNITY, 1998, 66 (04) :1755-1758
[6]   Regulation of WASP/WAVE proteins: making a long story short [J].
Bompard, G ;
Caron, E .
JOURNAL OF CELL BIOLOGY, 2004, 166 (07) :957-962
[7]   Mechanisms of WASp-mediated hematologic and immunologic disease [J].
Burns, S ;
Cory, GO ;
Vainchenker, W ;
Thrasher, AJ .
BLOOD, 2004, 104 (12) :3454-3462
[8]   Nck-independent actin assembly is mediated by two phosphorylated tyrosines within enteropathogenic Escherichia coli Tir [J].
Campellone, KG ;
Leong, JM .
MOLECULAR MICROBIOLOGY, 2005, 56 (02) :416-432
[9]   EspFU is a translocated EHEC effector that interacts with Tir and N-WASP and promotes nck-independent actin assembly [J].
Campellone, KG ;
Robbins, D ;
Leong, JM .
DEVELOPMENTAL CELL, 2004, 7 (02) :217-228
[10]   Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly [J].
Campellone, KG ;
Rankin, S ;
Pawson, T ;
Kirschner, MW ;
Tipper, DJ ;
Leong, JM .
JOURNAL OF CELL BIOLOGY, 2004, 164 (03) :407-416