Nck-independent actin assembly is mediated by two phosphorylated tyrosines within enteropathogenic Escherichia coli Tir
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.2005.04558.x/fullpdf
Reference40 articles.
1. The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network;Bladt;Mol Cell Biol,2003
2. Tails of two Tirs: actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7;Campellone;Curr Opin Microbiol,2003
3. A tyrosine-phosphorylated 12-amino-acid sequence of enteropathogenic Escherichia coli Tir binds the host adaptor protein Nck and is required for Nck localization to actin pedestals;Campellone;Mol Microbiol,2002
4. Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly;Campellone;J Cell Biol,2004a
5. EspFU is a translocated EHEC effector that interacts with Tir and N-WASP and promotes Nck-independent actin assembly;Campellone;Dev Cell,2004b
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