JCB logo
Carestream Gel Logic 212PRO
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text
Right arrow Full Text (PDF, 907K)
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 Belkin, A. M.
Right arrow Articles by Tarone, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Belkin, A. M.
Right arrow Articles by Tarone, G.
Right arrowPubmed/NCBI databases
*Substance via MeSH
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?

J. Cell Biol.
© The Rockefeller University Press
0021-9525/97/12/1583/13 $2.00
Volume 139, Number 6, December 15, 1997 1583-1595

Muscle beta 1D Integrin Reinforces the Cytoskeleton-Matrix Link: Modulation of Integrin Adhesive Function by Alternative Splicing

Alexey M. Belkin,* S. Francesco Retta,Dagger Dagger Dagger Olga Y. Pletjushkina,§ Fiorella Balzac,Dagger Lorenzo Silengo,Dagger Reinhard Fassler,par Victor E. Koteliansky, Keith Burridge,* and Guido TaroneDagger **

* Department of Cell Biology and Anatomy, University of North Carolina at Chapel Hill, North Carolina 27599; Dagger  Department of Biology, Genetics and Medical Chemistry, University of Torino, 10126 Torino, Italy; § Belozersky Institute of Physico-Chemical Biology, Moscow State University, 117311 Moscow, Russia; par  Max-Planck-Institute for Biochemistry, Martinsried D-82152, Germany;  Biogen Inc., Cambridge, Massachusetts 02142; ** Department of Psychology, University of Rome, Italy; and Dagger Dagger  Institute of Biology, University of Palermo, 90133 Palermo, Italy

Expression of muscle-specific beta 1D integrin with an alternatively spliced cytoplasmic domain in CHO and GD25, beta 1 integrin-minus cells leads to their phenotypic conversion. beta 1D-transfected nonmuscle cells display rounded morphology, lack of pseudopodial activity, retarded spreading, reduced migration, and significantly enhanced contractility compared with their beta 1A-expressing counterparts. The transfected beta 1D is targeted to focal adhesions and efficiently displaces the endogenous beta 1A and alpha vbeta 3 integrins from the sites of cell-matrix contact. This displacement is observed on several types of extracellular matrix substrata and leads to elevated stability of focal adhesions in beta 1D transfectants. Whereas a significant part of cellular beta 1A integrin is extractable in digitonin, the majority of the transfected beta 1D is digitonin-insoluble and is strongly associated with the detergent-insoluble cytoskeleton. Increased interaction of beta 1D integrin with the actin cytoskeleton is consistent with and might be mediated by its enhanced binding to talin. In contrast, beta 1A interacts more strongly with alpha -actinin, than beta 1D. Inside-out driven activation of the beta 1D ectodomain increases ligand binding and fibronectin matrix assembly by beta 1D transfectants. Phenotypic effects of beta 1D integrin expression in nonmuscle cells are due to its enhanced interactions with both cytoskeletal and extracellular ligands. They parallel the transitions that muscle cells undergo during differentiation. Modulation of beta 1 integrin adhesive function by alternative splicing serves as a physiological mechanism reinforcing the cytoskeleton- matrix link in muscle cells. This reflects the major role for beta 1D integrin in muscle, where extremely stable association is required for contraction.


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