JCB logo
Track the topics, authors and articles important to you
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 20 December 2004. doi:10.1083/jcb.200404100
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 6, 1231-1240
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
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 Yang, X.
Right arrow Articles by Hemler, M. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yang, X.
Right arrow Articles by Hemler, M. E.
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

 Palmitoylation supports assembly and function of integrin–tetraspanin complexes

Xiuwei Yang, Oleg V. Kovalenko, Wei Tang, Christoph Claas, Christopher S. Stipp, and Martin E. Hemler

Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115

Correspondence to Martin E. Hemler: Martin_Hemler{at}dfci.harvard.edu

As observed previously, tetraspanin palmitoylation promotes tetraspanin microdomain assembly. Here, we show that palmitoylated integrins ({alpha}3, {alpha}6, and ß4 subunits) and tetraspanins (CD9, CD81, and CD63) coexist in substantially overlapping complexes. Removal of ß4 palmitoylation sites markedly impaired cell spreading and signaling through p130Cas on laminin substrate. Also in palmitoylation-deficient ß4, secondary associations with tetraspanins (CD9, CD81, and CD63) were diminished and cell surface CD9 clustering was decreased, whereas core {alpha}6ß4–CD151 complex formation was unaltered. There is also a functional connection between CD9 and ß4 integrins, as evidenced by anti-CD9 antibody effects on ß4-dependent cell spreading. Notably, ß4 palmitoylation neither increased localization into "light membrane" fractions of sucrose gradients nor decreased solubility in nonionic detergents—hence it does not promote lipid raft association. Instead, palmitoylation of ß4 (and of the closely associated tetraspanin CD151) promotes CD151–{alpha}6ß4 incorporation into a network of secondary tetraspanin interactions (with CD9, CD81, CD63, etc.), which provides a novel framework for functional regulation.

Abbreviations used in this paper: EGFR, EGF receptor; TEM, tetraspanin-enriched microdomain.


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