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MBC in Press, published online ahead of print June 13, 2003
Mol. Biol. Cell 10.1091/mbc.E02-12-0824

A more recent version of this article appeared on September 1, 2003
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Submitted on December 15, 2002
Revised on May 16, 2003
Accepted on May 18, 2003

The {beta}1 Cytoplasmic Domain Regulates the Laminin-Binding Specificity of the {alpha}7X1 Integrin

Ming-Guang Yeh1, Barry L. Ziober1, Baomei Liu1, Galina Lipkina1, Ioannis Vizirianakis1, and Randall H. Kramer1*

1 Department of Stomatology and Department of Anatomy, University of California at San Francisco, San Francisco, CA 94143-0512, Present address: Department of Otorhinolaryngology, University of Pennsylvania, Philadelphia, PA 19104. Present address: Laboratory of Pharmacology, Department of Pharmaceutical Sciences, Aristotle University of Thessaloniki, GR-54006, Thessaloniki, Greece

* Corresponding author. E-mail address: rkramer{at}itsa.ucsf.edu.

During muscle development, the laminin-specific {alpha}7 integrin is alternatively spliced in the putative ligand-binding domain to yield either the {alpha}7X1 or the {alpha}7X2 variant. Following differentiation, {alpha}7X2 becomes the dominant form. Similarly, the partner {beta}1 integrin cytoplasmic domain is converted from the {beta}1A to the {beta}1D splice variant. To determine whether {beta}1D modulates the activity of the {alpha}7 receptor, cells were transfected with {alpha}7X1 and {beta}1D cDNA. {alpha}7X1 coupled with {beta}1A failed to adhere to laminin-1, whereas cotransfectants expressing {alpha}7X1 and {beta}1D showed strong adhesion. Attachment to other ligands was not significantly altered. Interestingly, {alpha}7X1 whether complexed with {beta}1A or {beta}1D displayed the same level of poor adhesion to laminin-2/4 or strong adhesion to laminin-10/11. These findings indicate that {alpha}7 function is regulated not only by X1/X2 in its extracellular domain but also by {beta}1 cytoplasmic splice variants. It is likely that expression of {beta}1D alters {alpha}7X1 binding to laminin isoforms by a process related to ligand affinity modulation. Functional regulation of {alpha}7{beta}1 by developmentally regulated splicing events may be important during myogenic differentiation and repair as the integrin mediates adhesion, motility, and cell survival.




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J. Liu, P. B. Gurpur, and S. J. Kaufman
Genetically Determined Proteolytic Cleavage Modulates {alpha}7{beta}1 Integrin Function
J. Biol. Chem., December 19, 2008; 283(51): 35668 - 35678.
[Abstract] [Full Text] [PDF]


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