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(Journal of Leukocyte Biology. 2002;72:199-206.)
© 2002 by Society for Leukocyte Biology

Differential localization of IL-2- and -15 receptor chains in membrane rafts of human T cells

Jens Goebel^*, Kathy Forrest^*, Lorri Morford and Thomas L. Roszman

^* Departments of Pediatrics and
Immunology, University of Kentucky Medical Center, Lexington

Correspondence: Jens Goebel, M.D., Section of Pediatric Nephrology, Room J455, Kentucky Clinic Building, Department of Pediatrics, University of Kentucky, Lexington, KY 40536-0284. E-mail: jwgoeb0{at}uky.edu

We studied whether cytokine receptors (Rs) on T cells associate with lipid microdomains ("rafts"). Low-dose phytohemagglutinin (PHA)-stimulated human T cells were separated into cytoplasmic, membrane, and raft fractions by buoyant density centrifugation. Examination of these fractions for the presence of interleukin (IL)-2- and -15R chains and associated signaling molecules by Western blotting revealed marked, selective enrichment of the IL-2/15R ß-chain in rafts before IL-2 stimulation. After IL-2 stimulation, a substantial amount of the ß-chain was found in the membrane fraction. This partial translocation was also observed for the ß-chain-associated molecules JAK-1, p56^lck, and grb-2. Finally, raft disruption with methyl-ß-cyclodextrin (MBCD) attenuated IL-2-induced tyrosine phosphorylation events and selectively decreased the surface expression of the IL-2/15R ß-chain detected by flow cytometry. These results show that the IL-2/15R ß-chain is enriched in rafts obtained from low-dose, PHA-stimulated T cells, that IL-2 binding alters this enrichment, and that this enrichment may be functionally relevant as a possible mechanism to ensure cytokine selectivity and specificity.

Key Words: T lymphocytes • signal transduction • cytokine receptors

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