Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 98, Issue 22, Pages 12462-12467Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.221463098
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Funding
- NCI NIH HHS [K01 CA096706] Funding Source: Medline
- NHLBI NIH HHS [P50 HL054500, P01 HL040387, HL40387, HL54500] Funding Source: Medline
- NIDDK NIH HHS [R01 DK039806, DK39806] Funding Source: Medline
- NIGMS NIH HHS [F32 GM020806] Funding Source: Medline
- PHS HHS [FM20806] Funding Source: Medline
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Integrins are a family of alpha/beta heterodimeric membrane proteins, which mediate cell-cell and cell-matrix interactions. The molecular mechanisms by which integrins are activated and cluster are currently poorly understood. One hypothesis posits that the cytoplasmic tails of the alpha and beta subunits interact strongly with one another in a 1:1 interaction, and that this interaction is modulated in the course of the activation of alpha IIb beta3 [Hughes, P. E., et al. (1996) J. Biol. Chem. 271, 6571-6574]. To examine the structural basis for this interaction, protein fragments encompassing the transmembrane elix plus cytoplasmic tails of the alpha and beta subunits of alpha IIb beta3 were expressed and studied in phospholipid micelles at physiological salt concentrations. Analyses of these fragments by analytical ultracentrifugation, NMR, circular dichroism, and electrophoresis indicated that they had very little or no tendency to interact with one another. Instead, they formed homomeric interactions, with the alpha- and beta -fragments forming dimers and trimers, respectively. Thus, these regions of the protein structure may contribute to the clustering of integrins that accompanies cellular adhesion.
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