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© The Rockefeller University Press, 0021-9525/1999//673 $5.00
The Journal of Cell Biology, Volume 146, Number 3, , 1999 673-682

Original Article

Role of Cholesterol in Formation and Function of a Signaling Complex Involving {alpha}vβ3, Integrin-Associated Protein (Cd47), and Heterotrimeric G Proteins



Jennifer M. Greena, Alexander Zhelesnyakb, Jun Chungc, Frederik P. Lindbergb, Marika Sarfatid, William A. Frazierc, and Eric J. Browna

a Center for Host/Pathogen Interactions, University of California, San Francisco, San Francisco, California 94143
b Division of Infectious Diseases, Washington University School of Medicine, St. Louis, Missouri 63110
c Department of Biochemistry, Washington University School of Medicine, St. Louis, Missouri 63110
d Centre Hospitalier Universite de Montreal (CHUM), Montreal, Canada H2L 4M1
Center for Host/Pathogen Interactions, University of California, San Francisco, HSE 201, Campus Box 0513, 513 Parnassus Avenue, San Francisco, CA 94143-0513.(415) 514-0169(415) 514-0167

ebrown{at}medicine.ucsf.edu

Integrin-associated protein (CD47) is a multiply membrane spanning member of the immunoglobulin superfamily that regulates some adhesion-dependent cell functions through formation of a complex with {alpha}vβ3 integrin and trimeric G proteins. Cholesterol is critical for the association of the three protein components of the supramolecular complex and for its signaling. The multiply membrane spanning domain of IAP is required for complex formation because it binds cholesterol. The supramolecular complex forms preferentially in glycosphingolipid-enriched membrane domains. Binding of mAb 10G2 to the IAP Ig domain, previously shown to be required for association with {alpha}vβ3, is affected by both the multiply membrane spanning domain and cholesterol. These data demonstrate that cholesterol is an essential component of the {alpha}vβ3/IAP/G protein signaling complex, presumably acting through an effect on IAP conformation.

Key Words: cholesterol • integrin • cell adhesion • plasma membrane • vitronectin

© 1999 The Rockefeller University Press

1.used in this paper: DIG, detergent-insoluble glycolipid domain; GPI, glycosylphosphatidylinositol; IAP, integrin-associated protein (CD47); MβCD, methyl-β-cyclodextrin; MMS, multiply membrane spanning; TSP, thrombospondin; Vn, vitronectin


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In Brief
J. Cell Biol. 1999 146: 1-2. [Full Text] [PDF]





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