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Published online 23 September 2002. doi:10.1083/jcb.200204056
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© The Rockefeller University Press, 0021-9525/2002/9/1299 $5.00
The Journal of Cell Biology, Volume 158, Number 7, September 30, 2002 1299-1309

Article

An extracellular site on tetraspanin CD151 determines {alpha}3 and {alpha}6 integrin–dependent cellular morphology



Alexander R. Kazarov, Xiuwei Yang, Christopher S. Stipp, Bantoo Sehgal and Martin E. Hemler

Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115

Address correspondence to Martin E. Hemler, Dana-Farber Cancer Institute, Rm D1430, 44 Binney St., Boston, MA 02115. Tel.: (617) 632-3410. Fax: (617) 632-2662. E-mail: martin_hemler{at}dfci.harvard.edu

The {alpha}3ß1 integrin shows strong, stoichiometric, direct lateral association with the tetraspanin CD151. As shown here, an extracellular CD151 site (QRD194–196) is required for strong (i.e., Triton X-100–resistant) {alpha}3ß1 association and for maintenance of a key CD151 epitope (defined by monoclonal antibody TS151r) that is blocked upon {alpha}3 integrin association. Strong CD151 association with integrin {alpha}6ß1 also required the QRD194–196 site and masked the TS151r epitope. For both {alpha}3 and {alpha}6 integrins, strong QRD/TS151r-dependent CD151 association occurred early in biosynthesis and involved {alpha} subunit precursor forms. In contrast, weaker associations of CD151 with itself, integrins, or other tetraspanins (Triton X-100–sensitive but Brij 96–resistant) were independent of the QRD/TS151r site, occurred late in biosynthesis, and involved mature integrin subunits. Presence of the CD151–QRD194–196->INF mutant disrupted {alpha}3 and {alpha}6 integrin–dependent formation of a network of cellular cables by Cos7 or NIH3T3 cells on basement membrane Matrigel and markedly altered cell spreading. These results provide definitive evidence that strong lateral CD151–integrin association is functionally important, identify CD151 as a key player during {alpha}3 and {alpha}6 integrin–dependent matrix remodeling and cell spreading, and support a model of CD151 as a transmembrane linker between extracellular integrin domains and intracellular cytoskeleton/signaling molecules.

Key Words: integrins; Matrigel; tetraspanin proteins; CD151 antigen; laminin


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