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J Biol Chem, Vol. 275, Issue 7, 5059-5064, February 18, 2000
From the Department of Vascular Biology, Scripps Research
Institute, La Jolla, California 92037
CD98 is a type II transmembrane protein involved
in neutral and basic amino acid transport and in cell fusion events.
CD98 was implicated in the function of integrin adhesion receptors by
its capacity to reverse suppression of integrin activation by isolated
integrin
Class- and Splice Variant-specific Association of CD98 with
Integrin
Cytoplasmic Domains*
§,
,
1A domains. Here we report that CD98
associates with integrin cytoplasmic domains with a unique integrin
class and splice variant specificity. In particular, CD98 interacted with the ubiquitous 1A but not the muscle-specific
splice variant, 1D, or leukocyte-specific
7 cytoplasmic domains. The ability of CD98 to associate
with integrin cytoplasmic domains correlated with its capacity to
reverse suppression of integrin activation. The association of CD98
with integrin 1A cytoplasmic domains may regulate the
function and localization of these membrane proteins.
*
This work was supported in part by Grants HL48728 and
AR27214 from the National Institutes of Health. This is publication 12537-VB from the Scripps Research Institute.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.
Fellow of the National Kidney Foundation.
§
These authors contributed equally to this work.
¶
Supported by United States Army Medical Research and
Material Command Grant DAMD 17-97-1-7056.
Wellcome Trust International Prize Traveling Fellow.
**
Supported by a National Service Research Award
IF32HL 09922-01.
To whom correspondence should be addressed: Dept. of Vascular
Biology, Scripps Research Inst., 10550 N. Torrey Pines Rd., La Jolla,
CA 92037. Tel.: 619-784-7143; Fax: 619-784-7343; E-mail: ginsberg@
scripps.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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