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Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.
Umeå University, Faculty of Medicine, Department of Medical Biosciences.
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
2002 (English)In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 269, no 13, 3279-3288 p.Article in journal (Refereed) Published
Abstract [en]

This study addresses the interactions between the adaptor protein Shb and components involved in T cell signalling, including SLP-76, Gads, Vav and ZAP70. We show that both SLP-76 and ZAP70 co-immunoprecipitate with Shb in Jurkat T cells and that Shb and Vav co-immunoprecipitate when cotransfected in COS cells. We also demonstrate, utilizing fusion protein constructs, that SLP-76, Gads and Vav associate independently of each other to different domains or regions, of Shb. Overexpression of an SH2 domain-defective Shb causes diminished phosphorylation of SLP-76 and Vav and consequently decreased activation of c-Jun kinase upon T cell receptor (TCR) stimulation. Shb was also found to localize to glycolipid-enriched membrane microdomains (GEMs), also called lipid rafts, after TCR stimulation. Our results indicate that upon TCR stimulation, Shb is targeted to these lipid rafts where Shb aids in recruiting the SLP-76-Gads-Vav complex to the T cell receptor zeta-chain and ZAP70.

Place, publisher, year, edition, pages
2002. Vol. 269, no 13, 3279-3288 p.
URN: urn:nbn:se:umu:diva-33161PubMedID: 12084069OAI: diva2:310255
Available from: 2010-04-13 Created: 2010-04-13 Last updated: 2010-04-21Bibliographically approved

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Lindholm, Cecilia KHenriksson, Maria LHallberg, BengtWelsh, Michael
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