β1 Integrins Show Specific Association with CD98 Protein in Low Density Membranes

β1 Integrins Show Specific Association with CD98 Protein in Low Density Membranes

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β1 Integrins Show Specific Association with CD98 Protein in Low Density Membranes

dc.contributor.author	Kolesnikova, Tatiana V
dc.contributor.author	Mannion, Brian A
dc.contributor.author	Berditchevski, Fedor
dc.contributor.author	Hemler, Martin Edward
dc.date.accessioned	2012-03-11T01:28:40Z
dc.date.issued	2001
dc.identifier.citation	Kolesnikova, Tatiana V., Brian A. Mannion, Fedor Berditchevski, and Martin E. Hemler. 2001. β1 integrins show specific association with CD98 protein in low density membranes. BMC Biochemistry 2: 10.	en_US
dc.identifier.issn	1471-2091	en_US
dc.identifier.uri	http://nrs.harvard.edu/urn-3:HUL.InstRepos:8347346
dc.description.abstract	Background: The CD98 (4F2, FRP-1) is a widely expressed cell surface protein heterodimer composed of a glycosylated heavy chain and a non-glycosylated light chain. Originally described as a T cell activation antigen, it was later shown to function in amino acid transport, cell fusion and homotypic cell aggregation. Several lines of evidence suggest its functional interaction with integrins but the biochemical basis for this interaction has been unclear. Results: We demonstrate that CD98 constitutively and specifically associates with β1 integrins (α2β1,α3β1, α5β1 and α6β1), but minimally with α4β1. Integrin-CD98 association was established by reciprocal immunoprecipitation experiments, and confirmed by CD98-induced clustering of α3β1 but not α4β1 on the surface of rhabdomyosarcoma cells. Integrin-CD98 association is independent of the α subunit cytoplasmic tail, is maintained in α3β1 ligand-interaction deficient mutants, and is not inhibited by EDTA. Within the CD98 heavy chain, a C109S mutation (but not a C330S mutation) caused a loss of β1 integrin association. The same C109S mutation also caused a loss of CD98 light chain association. Importantly, CD98 associated selectively with β1 integrins present in low density "light membrane" fractions on a sucrose gradient. CD98 was not present in dense fractions that contained the majority of β1 integrins. Notably, the C109S mutant of CD98, that did not associate with β1 integrins, showed also a reduced localization into light membrane fractions. Conclusions: We demonstrate that CD98 association with β1 integrins is specific, occurs in the context of low density membranes, and may require the CD98 light chain.	en_US
dc.language.iso	en_US	en_US
dc.publisher	BioMed Central	en_US
dc.relation.isversionof	doi://10.1186/1471-2091-2-10	en_US
dc.relation.hasversion	http://www.ncbi.nlm.nih.gov/pmc/articles/PMC59658/pdf/	en_US
dash.license	LAA
dc.title	β1 Integrins Show Specific Association with CD98 Protein in Low Density Membranes	en_US
dc.type	Journal Article	en_US
dc.description.version	Version of Record	en_US
dc.relation.journal	BMC Biochemistry	en_US
dash.depositing.author	Hemler, Martin Edward
dc.date.available	2012-03-11T01:28:40Z
dash.affiliation.other	HMS^Pathology	en_US