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J Biol Chem, Vol. 273, Issue 45, 29424-29429, November 6, 1998

Molecular Characterization of the Signal Responsible for the Targeting of the Interleukin 2 Receptor beta  Chain toward Intracellular Degradation

Agathe Subtil, Anna Rocca, and Alice Dautry-Varsat

From Unité de Biologie des Interactions Cellulaires, URA CNRS 1960, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France

During receptor-mediated endocytosis, most growth factor receptors are transported to late endocytic compartments and degraded. This process is important to control their expression on the cell surface and requires sorting in early endocytic compartments. Little is known about the mechanisms and the signals involved. We have studied the signal involved in targeting the interleukin 2 receptor beta  chain (IL2Rbeta ), a member of the cytokine receptor superfamily, toward degradation after internalization. We show that a motif of 8 amino acids in the cytosolic tail of IL2Rbeta is sufficient to target a normally recycling receptor toward degradation. Deletion of this signal strongly impairs IL2Rbeta degradation. Further molecular characterization of the motif shows that it does not resemble the well documented tyrosine and dileucine families of trafficking signals.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.



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