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XB-ART-4015
J Cell Biol. February 2, 2004; 164 (3): 407-16.

Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly.

Campellone KG , Rankin S , Pawson T , Kirschner MW , Tipper DJ , Leong JM .


Abstract
Enteropathogenic Escherichia coli (EPEC) translocates effector proteins into mammalian cells to promote reorganization of the cytoskeleton into filamentous actin pedestals. One effector, Tir, is a transmembrane receptor for the bacterial surface adhesin intimin, and intimin binding by the extracellular domain of Tir is required for actin assembly. The cytoplasmic NH2 terminus of Tir interacts with focal adhesion proteins, and its tyrosine-phosphorylated COOH terminus binds Nck, a host adaptor protein critical for pedestal formation. To define the minimal requirements for EPEC-mediated actin assembly, Tir derivatives were expressed in mammalian cells in the absence of all other EPEC components. Replacement of the NH2 terminus of Tir with a viral membrane-targeting sequence promoted efficient surface expression of a COOH-terminal Tir fragment. Artificial clustering of this fusion protein revealed that the COOH terminus of Tir, by itself, is sufficient to initiate a complete signaling cascade leading to pedestal formation. Consistent with this finding, clustering of Nck by a 12-residue Tir phosphopeptide triggered actin tail formation in Xenopus egg extracts.

PubMed ID: 14757753
PMC ID: PMC2172230
Article link: J Cell Biol.
Grant support: R01-AI46454 NIAID NIH HHS

Genes referenced: actn1 actr3 aicda nck1 nck2 was wasl
Antibodies referenced:
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