JCB logo
BioLegend: Antibody Reagents
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online September 17, 2007
doi:10.1083/jcb.200703092
The Journal of Cell Biology, Vol. 178, No. 7, 1251-1264
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Okreglak et al.
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 Okreglak, V.
Right arrow Articles by Drubin, D. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Okreglak, V.
Right arrow Articles by Drubin, D. G.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene
*Substance via MeSH
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

 Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state

Voytek Okreglak and David G. Drubin

Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720

Correspondence to David G. Drubin: drubin{at}berkeley.edu

Cofilin is the major mediator of actin filament turnover in vivo. However, the molecular mechanism of cofilin recruitment to actin networks during dynamic actin-mediated processes in living cells and cofilin's precise in vivo functions have not been determined. In this study, we analyzed the dynamics of fluorescently tagged cofilin and the role of cofilin-mediated actin turnover during endocytosis in Saccharomyces cerevisiae. In living cells, cofilin is not necessary for actin assembly on endocytic membranes but is recruited to molecularly aged adenosine diphosphate actin filaments and is necessary for their rapid disassembly. Defects in cofilin function alter the morphology of actin networks in vivo and reduce the rate of actin flux through actin networks. The consequences of decreasing actin flux are manifested by decreased but not blocked endocytic internalization at the plasma membrane and defects in late steps of membrane trafficking to the vacuole. These results suggest that cofilin-mediated actin filament flux is required for the multiple steps of endocytic trafficking.

Abbreviations used in this paper: CPY, carboxypeptidase Y; F-actin, filamentous actin; lat A, latrunculin A; mRFP, monomeric RFP; SD, synthetic dextrose; TRP, tryptophan; vps, vacuolar protein sorting.


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