JCB logo
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online
doi:10.1083/jcb.200811116
The Journal of Cell Biology, Vol. 185, No. 6, 1097-1110
The Rockefeller University Press, 0021-9525 $30.00
© Burston et al.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 6855K)
Right arrow PDF+supp data (10947K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material
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 CrossRef
Google Scholar
Right arrow Articles by Burston, H. E.
Right arrow Articles by Conibear, E.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Burston, H. E.
Right arrow Articles by Conibear, E.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Article

Regulators of yeast endocytosis identified by systematic quantitative analysis



Helen E. Burston1,2, Lymarie Maldonado-Báez3, Michael Davey1,2, Benjamen Montpetit1,2, Cayetana Schluter1,2, Beverly Wendland3, and Elizabeth Conibear1,2

1 Centre for Molecular Medicine and Therapeutics, Child and Family Research Institute, and 2 Department of Medical Genetics, University of British Columbia, Vancouver V5Z 4H4, British Columbia, Canada
3 Department of Biology, The Johns Hopkins University, Baltimore, MD 21218

Correspondence to Elizabeth Conibear: conibear{at}cmmt.ubc.ca

Endocytosis of receptors at the plasma membrane is controlled by a complex mechanism that includes clathrin, adaptors, and actin regulators. Many of these proteins are conserved in yeast yet lack observable mutant phenotypes, which suggests that yeast endocytosis may be subject to different regulatory mechanisms. Here, we have systematically defined genes required for internalization using a quantitative genome-wide screen that monitors localization of the yeast vesicle-associated membrane protein (VAMP)/synaptobrevin homologue Snc1. Genetic interaction mapping was used to place these genes into functional modules containing known and novel endocytic regulators, and cargo selectivity was evaluated by an array-based comparative analysis. We demonstrate that clathrin and the yeast AP180 clathrin adaptor proteins have a cargo-specific role in Snc1 internalization. We additionally identify low dye binding 17 (LDB17) as a novel conserved component of the endocytic machinery. Ldb17 is recruited to cortical actin patches before actin polymerization and regulates normal coat dynamics and actin assembly. Our findings highlight the conserved machinery and reveal novel mechanisms that underlie endocytic internalization.

Abbreviations used in this paper: CALM, clathrin assembly lymphoid myeloid leukemia; LatA, latrunculin A; Ldb17, low dye binding 17; ORF, open reading frame; PRD, proline-rich domain; VAMP, vesicle-associated membrane protein; WASP, Wiscott-Aldrich syndrome protein.

© 2009 Burston et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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 Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




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