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© The Rockefeller University Press, 0021-9525/1999//477 $5.00
The Journal of Cell Biology, Volume 146, Number 2, , 1999 477-492

Characterization of Integrin–Tetraspanin Adhesion Complexes

Fedor Berditchevski^a and Elena Odintsova^a

^a CRC Institute for Cancer Studies, The University of Birmingham, Edgbaston, Birmingham, United Kingdom B15 2TA
CRC Institute for Cancer Studies, The University of Birmingham, Egdbaston, Birmingham, B15 2TA, United Kingdom.44-121-414 448644-121-414 7458

f.berditchevski{at}bham.ac.uk

Tetraspanins (or proteins from the transmembrane 4 superfamily, TM4SF) form membrane complexes with integrin receptors and are implicated in integrin-mediated cell migration. Here we characterized cellular localization, structural composition, and signaling properties of 3β1–TM4SF adhesion complexes. Double-immunofluorescence staining showed that various TM4SF proteins, including CD9, CD63, CD81, CD82, and CD151 are colocalized within dot-like structures that are particularly abundant at the cell periphery. Differential extraction in conjunction with chemical cross-linking indicated that the cell surface fraction of 3β1–TM4SF protein complexes may not be directly linked to the cytoskeleton. However, in cells treated with cytochalasin B 3β1–TM4SF protein complexes are relocated into intracellular vesicles suggesting that actin cytoskeleton plays an important role in the distribution of tetraspanins into adhesion structures. Talin and MARCKS are partially codistributed with TM4SF proteins, whereas vinculin is not detected within the tetraspanin-containing adhesion structures. Attachment of serum-starved cells to the immobilized anti-TM4SF mAbs induced dephosphorylation of focal adhesion kinase (FAK). On the other hand, clustering of tetraspanins in cells attached to collagen enhanced tyrosine phosphorylation of FAK. Furthermore, ectopic expression of CD9 in fibrosarcoma cells affected adhesion-induced tyrosine phosphorylation of FAK, that correlated with the reorganization of the cortical actin cytoskeleton. These results show that tetraspanins can modulate integrin signaling, and point to a mechanism by which TM4SF proteins regulate cell motility.

Key Words: integrin • tetraspanin • adhesion complexes • signaling • cytoskeleton

© 1999 The Rockefeller University Press

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