JCB logo
BioLegend: Antibody Reagents
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 4 December 2006. doi:10.1083/jcb.200604046
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 175, Number 5, 803-813
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
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 Hanono, A.
Right arrow Articles by Bretscher, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hanono, A.
Right arrow Articles by Bretscher, A.
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

 EPI64 regulates microvillar subdomains and structure

Abraham Hanono, Damien Garbett, David Reczek, David N. Chambers, and Anthony Bretscher

Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853

Correspondence to Anthony Bretscher: apb5{at}cornell.edu

EPI64 is a TBC domain–containing protein that binds the PDZ domains of EBP50, which binds ezrin, a major actin-binding protein of microvilli. High-resolution light microscopy revealed that ezrin and EBP50 localize exclusively to the membrane-surrounded region of microvilli, whereas EPI64 localizes to variable regions in the structures. Overexpressing EPI64 results in its and EBP50's relocalization to the base of microvilli, including to the actin rootlet devoid of ezrin or plasma membrane. Uncoupling EPI64's binding to EBP50, expression of any construct mislocalizing its TBC domain, or knock down of EBP50 results in loss of microvilli. The TBC domain of EPI64 binds directly to Arf6-GTP. Overexpressing the TBC domain increases Arf6-GTP levels, and expressing dominant-active Arf6 results in microvillar loss. These data reveal that microvilli have distinct cytoskeletal subdomains and that EPI64 regulates microvillar structure.

D. Reczek's present address is Genzyme Corporation, Framingham, MA 01701.

D.N. Chamber's present address is Department of Biology, Concord University, Athens, WV 24712.

Abbreviations used in this paper: C-ERMAD, C-terminal ERM association domain; EBP50, ERM binding phosphoprotein of 50 kD; EPI64, EBP50 PDZ interactor of 64 kD; ERM, ezrin/radixin/moesin; FERM, 4.1 ERM; PDZ, postsynaptic density/95-discs large/zona occludens-1; GAP, GTPase activating protein; TBC, Tre-2/Bub2/Cdc16.


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