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Originally published In Press as doi:10.1074/jbc.M108030200 on October 16, 2001

J. Biol. Chem., Vol. 276, Issue 52, 48764-48774, December 28, 2001
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Assembly of Glycoprotein-80 Adhesion Complexes in Dictyostelium
RECEPTOR COMPARTMENTALIZATION AND OLIGOMERIZATION IN MEMBRANE RAFTS*

Tony J. C. HarrisDagger §, Amir Ravandi§Dagger , and Chi-Hung SiuDagger §||

From the Dagger  Banting and Best Department of Medical Research and § Department of Biochemistry, University of Toronto, Toronto, Ontario M5G 1L6, Canada

The phospholipid-anchored membrane glycoprotein (gp)-80 mediates cell-cell adhesion through a homophilic trans-interaction mechanism during Dictyostelium development and is enriched in a Triton X-100-insoluble floating fraction. To elucidate how gp80 adhesion complexes assemble in the plasma membrane, gp80-gp80 and gp80-raft interactions were investigated. A low density raft-like membrane fraction was isolated using a detergent-free method. It was enriched in sterols, the phospholipid-anchored proteins gp80, gp138, and ponticulin, as well as DdCD36 and actin, corresponding to components found in the Triton X-100-insoluble floating fraction. Chemical cross-linking revealed that gp80 oligomers were enriched in the raft-like membrane fraction, implicating stable oligomer-raft interactions. However, gp80 oligomers resisted sterol sequestration and were partially dissociated with Triton X-100, suggesting that compartmentalization in rafts was not solely responsible for their formation. The trans-dimer known to mediate adhesion was identified, but cis-oligomerization predominated and displayed greater accumulation during development. In fact, oligomerization was dependent on the level of gp80 expression and occurred among isolated gp80 extracellular domains, indicating that it was mediated by direct gp80-gp80 interactions. Rafts existed in gp80-null cells and such pre-existent membrane domains may provide optimal microenvironments for gp80 cis-oligomerization and the assembly of adhesion complexes.

* This work was supported in part by Operating Grant MT-6140 from the Canadian Institutes of Health Research.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.

Recipient of a postgraduate scholarship from the Natural Sciences and Engineering Research Council of Canada and a University of Toronto Open Scholarship.

|| To whom correspondence should be addressed: Charles H. Best Institute, University of Toronto, 112 College Street, Toronto, Ontario M5G 1L6, Canada. Tel.: 416-978-8766; Fax: 416-978-8528; E-mail: chi.hung.siu@utoronto.ca.

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