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© The Rockefeller University Press, 0021-9525/1997//583 $5.00
The Journal of Cell Biology, Volume 136, Number 3, , 1997 583-595

Article

An {alpha}-Helical Signal in the Cytosolic Domain of the Interleukin 2 Receptor β Chain Mediates Sorting Towards Degradation after Endocytosis



Agathe Subtil, Muriel Delepierre*, and Alice Dautry-Varsat

Unité de Biologie des Interactions Cellulaires, URA CNRS 1960, and * Laboratoire de Résonance Magnétique Nucléaire, URA CNRS 1129, Institut Pasteur, 75724 Paris Cedex 15, France

High-affinity IL2 receptors consist of three components, the {alpha}, β, and {gamma} chains that are associated in a noncovalent manner. Both the β and {gamma} chains belong to the cytokine receptor superfamily. Interleukin 2 (IL2) binds to high-affinity receptors on the cell surface and IL2-receptor complexes are internalized. After endocytosis, the components of this multimolecular receptor have different intracellular fates: one of the chains, {alpha}, recycles to the plasma membrane, while the others, β and {gamma}, are routed towards late endocytic compartments and are degraded. We show here that the cytosolic domain of the β chain contains a 10–amino acid sequence which codes for a sorting signal. When transferred to a normally recycling receptor, this sequence diverts it from recycling. The structure of a 17–amino acid segment of the β chain including this sequence has been studied by nuclear magnetic resonance and circular dichroism spectroscopy, which revealed that the 10 amino acids corresponding to the sorting signal form an amphipathic {alpha} helix. This work thus describes a novel, highly structured signal, which is sufficient for sorting towards degradation compartments after endocytosis.

Abbreviations used in this paper: CD, circular dichroism; IL2, interleukin 2; NOE, nuclear Overhauser effect; NOESY, two-dimensional NOE spectroscopy; NMR, nuclear magnetic resonance; ROESY, rotating frame NOE; TFE, trifluoroethanol; TOCSY, total correlation spectroscopy.

We greatly appreciate the help of Dr. Agnès Hémar at the beginning of this work. We are grateful to Dr. H. Gahery for helping with initial β constructs, to E. Gilard for helping with NMR analyses, to Drs. C. Bonnerot, P. Cosson, and T. Kono for providing plasmids NT, T-XO and pdKCRβ, respectively, and to Dr. R. Robb for the gift of antibodies 341 and 561. We are grateful to Drs. Anne Lecroisey, Sebastian Amigorena, Emmanuel Morelon, and David Ojcius for critical reading of the manuscript.

Please address all correspondence to A. Dautry-Varsat, Unite de Biologie des Interactions Cellulaires, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris Cedex 15, France. Tel.: 33 1 45 68 8574. Fax: 33 1 40 61 3238. E-mail: adautry{at}pasteur.fr


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