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PNAS 99 (1): 225-232

Copyright © 2002 by the National Academy of Sciences.

Inaugural Article


BIOLOGICAL SCIENCES / CELL BIOLOGY

The glycosynapse

Sen-itiroh Hakomori*

Pacific Northwest Research Institute, 720 Broadway, Seattle, WA 98122-4327, and Departments of Pathobiology and Microbiology, University of Washington, Seattle, WA 98195

Contributed by Sen-itiroh Hakomori

Accepted for publication October 11, 2001.

Abstract: Physically distinguishable microdomains associated with various functional membrane proteins are one of the major current topics in cell biology. Glycosphingolipids present in such microdomains have been used as "markers;" however, the functional role of glycosyl epitopes in microdomains has received little attention. In this review, I have tried to summarize the evidence that glycosyl epitopes in microdomains mediate cell adhesion and signal transduction events that affect cellular phenotypes. Molecular assemblies that perform such functions are hereby termed "glycosynapse" in analogy to "immunological synapse," the membrane assembly of immunocyte adhesion and signaling. Three types of glycosynapses are so far distinguishable: (i) Glycosphingolipids organized with cytoplasmic signal transducers and proteolipid tetraspanin with or without growth factor receptors; (ii) transmembrane mucin-type glycoproteins with clustered O-linked glycoepitopes for cell adhesion and associated signal transducers at lipid domain; and (iii) N-glycosylated transmembrane adhesion receptors complexed with tetraspanin and gangliosides, as typically seen with the integrin–tetraspanin–ganglioside complex. The possibility is discussed that glycosynapses give rise to a high degree of diversity and complexity of phenotypes.


* Division of Biomembrane Research, Pacific Northwest Research Institute, 720 Broadway, Seattle, WA 98122-4327. E-mail: hakomori{at}u.washington.edu.

This contribution is part of the special series of Inaugural Articles by members of the National Academy of Sciences elected on May 1, 2001.

{dagger} Glycosphingolipids are abbreviated according to the recommendations of the International Union of Pure and Applied Chemistry-International Union of Biochemistry Commission on Biochemical Nomenclature (CBN) [CBN for lipids (1977) Eur. J. Biochem. 79, 11–21]; however, the suffix -OseCer is omitted. Ganglio-series gangliosides are abbreviated according to the extended version of Svennerholm's list [Holmgren, J., Svennerholm, L., Elwing, H., Fredman, P. & Strannegard, O. (1980) Proc. Natl. Acad. Sci. USA 77, 1947–1950].

{ddagger} The term "glycosynapse" is applied to the membrane assembly involved in glycosylation-dependent cell adhesion and signaling, in analogy to "immunological synapse," which controls functional adhesion between immunocytes (refs. 120 and 121). The term supplements the concepts of "caveolae" (1), "raft" (5), and other terms which do not implicate glycosylation-dependent cell function.


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