Tyrosine phosphorylation is required for actin-based motility of vaccinia but not Listeria or Shigella

Studies of the actin-based motility of pathogens have provided important insights into the events occurring at the leading edge of motile cells [1–3]. To date, several actin-cytoskeleton-associated proteins have been implicated in the motility of Listeria or Shigella: vasodilator-stimulated phosphop...

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Bibliographic Details
Published in:Current biology 1999-01, Vol.9 (2), p.89,S1-92,S2
Main Authors: Frischknecht, Friedrich, Cudmore, Sally, Moreau, Violaine, Reckmann, Inge, Röttger, Sabine, Way, Michael
Format: Article
Language:English
Subjects:
Actins - metabolism
Actins - physiology
Chemotaxis
Fluorescent Antibody Technique
HeLa Cells
Humans
Listeria
Listeria - physiology
Listeria - ultrastructure
Microscopy, Immunoelectron
Phosphorylation
Shigella
Shigella - physiology
Shigella - ultrastructure
Tyrosine - metabolism
Vaccinia virus - physiology
Vaccinia virus - ultrastructure
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Summary:Studies of the actin-based motility of pathogens have provided important insights into the events occurring at the leading edge of motile cells [1–3]. To date, several actin-cytoskeleton-associated proteins have been implicated in the motility of Listeria or Shigella: vasodilator-stimulated phosphoprotein (VASP), vinculin and the actin-related protein complex of Arp2 and Arp3 [4–7]. To further investigate the underlying mechanism of actin-tail assembly, we examined the localization of components of the actin cytoskeleton including Arp3, VASP, vinculin and zyxin during vaccinia, Listeria and Shigella infections. The most striking difference between the systems was that a phosphotyrosine signal was observed only at the site of vaccinia actin-tail assembly. Micro-injection experiments demonstrated that a phosphotyrosine protein plays an important role in vaccinia actin-tail formation. In addition, we observed a phosphotyrosine signal on clathrin-coated vesicles that have associated actin-tail-like structures and on endogenous vesicles in Xenopus egg extracts which are able to nucleate actin tails [8,9]. Our observations indicate that a host phosphotyrosine protein is required for the nucleation of actin filaments by vaccinia and suggest that this phosphoprotein might be associated with cellular membranes that can nucleate actin.
ISSN:0960-9822
1879-0445
DOI:10.1016/S0960-9822(99)80020-7