HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 283, Issue 21, 14600-14609, May 23, 2008

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 283/21/14600    most recent M707818200v2 M707818200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Khan, A. A. Articles by Chishti, A. H. PubMed PubMed Citation Articles by Khan, A. A. Articles by Chishti, A. H. Social Bookmarking                      What's this?

Dematin and Adducin Provide a Novel Link between the Spectrin Cytoskeleton and Human Erythrocyte Membrane by Directly Interacting with Glucose Transporter-1^*

Anwar A. Khan, Toshihiko Hanada, Morvarid Mohseni, Jong-Jin Jeong, Lixiao Zeng, Massimiliano Gaetani, Donghai Li, Brent C. Reed^¶, David W. Speicher, and Athar H. Chishti¹

From the Department of Pharmacology, University of Illinois Cancer Center, University of Illinois College of Medicine, Chicago, Illinois 60612, Systems Biology Division, The Wistar Institute, Philadelphia, Pennsylvania 19104, and the ^¶Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, Louisiana 71130

Dematin and adducin are actin-binding proteins located at the spectrin-actin junctions, also called the junctional complex, in the erythrocyte membrane. Here we propose a new model whereby dematin and adducin link the junctional complex to human erythrocyte plasma membrane. Using a combination of surface labeling, immunoprecipitation, and vesicle proteomics approaches, we have identified glucose transporter-1 as the receptor for dematin and adducin in the human erythrocyte membrane. This finding is the first description of a transmembrane protein that binds to dematin and adducin, thus providing a rationale for the attachment of the junctional complex to the lipid bilayer. Because homologues of dematin, adducin, and glucose transporter-1 exist in many non-erythroid cells, we propose that a conserved mechanism may exist that couples sugar and other related transporters to the actin cytoskeleton.

Received for publication, September 18, 2007 , and in revised form, March 7, 2008.

^* This work was supported, in whole or in part, by National Institutes of Health Grants HL051445 (to A. H. C.) and HL38794 (to D. W. S.). This work was also supported by the American Heart Association, Southeast Affiliate, Award 0555389B (to B. C. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables 1 and 2.

¹ To whom correspondence should be addressed: University of Illinois Cancer Center, MC-704, 909 South Wolcott Ave., Chicago, IL 60612-3725. Tel.: 312-355-1293; E-mail: chishti{at}uic.edu.

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