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

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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

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