Direct Extracellular Contact between Integrin α3β1 and TM4SF Protein CD151*

By R. Yauch, A. Kazarov, B. Desai, Richard T. Lee, M. Hemler. Journal of Biological Chemistry, 2000

180 citations recorded by the source corpus.

Previously we established that the α3β1 integrin shows stable, specific, and stoichiometric association with the TM4SF (tetraspannin) protein CD151. Here we used a membrane impermeable cross-linking agent to show a direct association between extracellular domains of α3β1 and CD151. The α3β1−CD151 association site was then mapped using chimeric α6/α3 integrins and CD151/NAG2 TM4SF proteins. Complex formation required an extracellular α3 site (amino acids (aa) 570–705) not previously known to be involved in specific integrin contacts with other proteins and a region (aa 186–217) within the large extracellular loop of CD151. Notably, the anti-CD151 monoclonal antibody TS151r binding epitope, previously implicated in α3 integrin association, was mapped to the same region of CD151 (aa 186–217). Finally, we demonstrated that both NH2- and COOH-terminal domains of CD151 are located on the inside of the plasma membrane, thus confirming a long suspected model of TM4SF protein topology.

Subfields: Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/fb3ddbaf96746142e56d291abd1d2aa01fc74ee1

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In Molecular Biology

F. Berditchevski

Citations in the corpus

Complexes of tetraspanins with integrins: more than meets the eye. (2001, background): “Notably, corresponding mutations in α3 did not affect the association with CD151 (Yauch et al., 2000), which suggests that the interacting interfaces of the CD151-α3β1 and CD81-α4β1 complexes differ.”
Function of the Tetraspanin CD151–α6β1 Integrin Complex during Cellular Morphogenesis (2002, background): “A specific site in CD151’s large extracellular loop is required for 3 1 integrin interaction (Yauch et al., 2000).”