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Originally published In Press as doi:10.1074/jbc.M008650200 on December 11, 2000

J. Biol. Chem., Vol. 276, Issue 11, 7974-7984, March 16, 2001
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Evaluation of Prototype Transmembrane 4 Superfamily Protein Complexes and Their Relation to Lipid Rafts*

Christoph Claas, Christopher S. Stipp, and Martin E. HemlerDagger

From the Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115

Recent literature suggests that tetraspanin proteins (transmembrane 4 superfamily; TM4SF proteins) may associate with each other and with many other transmembrane proteins to form large complexes that sometimes may be found in lipid rafts. Here we show that prototype complexes of CD9 or CD81 (TM4SF proteins) with alpha 3beta 1 (an integrin) and complexes of CD63 (a TM4SF protein) with phosphatidylinositol 4-kinase (PtdIns 4-K) may indeed localize within lipid raft-like microdomains, as seen by three different criteria. First, these complexes localize to low density light membrane fractions in sucrose gradients. Second, CD9 and alpha 3 integrin colocalized with ganglioside GM1 as seen by double staining of fixed cells. Third, CD9-alpha 3beta 1 and CD81-alpha 3beta 1 complexes were shifted to a higher density upon cholesterol depletion from intact cells or cell lysate. However, CD9-alpha 3beta 1, CD81-alpha 3beta 1, and CD63-PtdIns 4-K complex formation itself was not dependent on localization into raftlike lipid microdomains. These complexes did not require cholesterol for stabilization, were maintained within well solubilized dense fractions from sucrose gradients, were stable at 37 °C, and were small enough to be included within CL6B gel filtration columns. In summary, prototype TM4SF protein complexes (CD9-alpha 3beta 1, CD81-alpha 3beta 1, and CD63-PtdIns 4-K) can be solubilized as discrete units, independent of lipid microdomains, although they do associate with microdomains resembling lipid rafts.

* This work was supported by National Institutes of Health Grants GM38903 and CA42368 and by Deutsche Forschungsgemeinschaft Grant Cl 163/1-1 (to C. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dana-Farber Cancer Institute, Rm. D-1430, 44 Binney St., Boston, MA 02115. Tel.: 617-632-3410; Fax: 617-632-2662; E-mail: Martin_Hemler@DFCI.Harvard.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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