JCB logo
Epitomics: The Rabbit Monoclonal Company
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online 8 August 2005. doi:10.1083/jcb.200502053
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 4, 637-648
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sirotkin, V.
Right arrow Articles by Pollard, T. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sirotkin, V.
Right arrow Articles by Pollard, T. D.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast

Vladimir Sirotkin1, Christopher C. Beltzner1, Jean-Baptiste Marchand4, and Thomas D. Pollard1,2,3

1 Departments of Molecular Cellular and Developmental Biology, Yale University, New Haven, CT 06520
2 Departments of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520
3 Departments of Cell Biology, Yale University, New Haven, CT 06520
4 Avidis, Biopole Clermont-Limagne, 63360 Saint Beauzire, France

Correspondence to Thomas D. Pollard: thomas.pollard{at}yale.edu

Yeast actin patches are dynamic structures that form at the sites of cell growth and are thought to play a role in endocytosis. We used biochemical analysis and live cell imaging to investigate actin patch assembly in fission yeast Schizosaccharomyces pombe. Patch assembly proceeds via two parallel pathways: one dependent on WASp Wsp1p and verprolin Vrp1p converges with another dependent on class 1 myosin Myo1p to activate the actin-related protein 2/3 (Arp2/3) complex. Wsp1p activates Arp2/3 complex via a conventional mechanism, resulting in branched filaments. Myo1p is a weaker Arp2/3 complex activator that makes unstable branches and is enhanced by verprolin. During patch assembly in vivo, Wsp1p and Vrp1p arrive first independent of Myo1p. Arp2/3 complex associates with nascent activator patches over 6–9 s while remaining stationary. After reaching a maximum concentration, Arp2/3 complex patches move centripetally as activator proteins dissociate. Genetic dependencies of patch formation suggest that patch formation involves cross talk between Myo1p and Wsp1p/Vrp1p pathways.

Abbreviations used in this paper: Arp2/3, actin-related protein 2/3; CA, central-acidic; mGFP, monomeric GFP; N-WASP, neuronal WASp; SH3, Src homology 3; TH, tail homology; WASp, Wiskott-Aldrich Syndrome protein; WH2, WASp homology 2.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents