JCB logo
AbD Serotec: www.ab-direct.com/4for3
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 21 November 2005. doi:10.1083/jcb.200504016
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 4, 705-715
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 Fagerholm, S. C.
Right arrow Articles by Gahmberg, C. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fagerholm, S. C.
Right arrow Articles by Gahmberg, C. G.
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

 Specific integrin {alpha} and ß chain phosphorylations regulate LFA-1 activation through affinity-dependent and -independent mechanisms

Susanna C. Fagerholm, Tiina J. Hilden, Susanna M. Nurmi, and Carl G. Gahmberg

Division of Biochemistry, Faculty of Biosciences, University of Helsinki, FIN-00014 Helsinki, Finland

Correspondence to Carl G. Gahmberg: carl.gahmberg{at}helsinki.fi

Integrins are adhesion receptors that are crucial to the functions of multicellular organisms. Integrin-mediated adhesion is a complex process that involves both affinity regulation and cytoskeletal coupling, but the molecular mechanisms behind this process have remained incompletely understood. In this study, we report that the phosphorylation of each cytoplasmic domain of the leukocyte function-associated antigen-1 integrin mediates different modes of integrin activation. {alpha} Chain phosphorylation on Ser1140 is needed for conformational changes in the integrin after chemokine- or integrin ligand–induced activation or after activation induced by active Rap1 (Rap1V12). In contrast, the ß chain Thr758 phosphorylation mediates selective binding to 14-3-3 proteins in response to inside-out activation through the T cell receptor, resulting in cytoskeletal rearrangements. Thus, site-specific phosphorylation of the integrin cytoplasmic domains is important for the dynamic regulation of these complex receptors in cells.

S.C. Fagerholm and T.J. Hilden contributed equally to this paper.

Abbreviations used in this paper: ICAM, intercellular adhesion molecule; J, Jurkat; LFA-1, leukocyte function-associated antigen-1; sICAM, soluble ICAM; TCR, T cell receptor; wt, wild-type.


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