A Restricted Cytoplasmic Region of IL-2 Receptor Beta Chain is Essential for Growth Signal Transduction but Not for Ligand Binding and Internalization

Overview

Journal Cell

Publisher Cell Press

Specialty Cell Biology

Date 1989 Dec 1

PMID 2590941

Citations 105

Authors

M Hatakeyama

H Mori

T Doi

T Taniguchi

Affiliations

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Abstract

The functional, high affinity form of interleukin-2 receptor (IL-2R) is composed of two receptor components, the IL-2R alpha (p55) and IL-2R beta (p70-75) chains. Unlike the IL-2R alpha chain, the IL-2R beta chain contains a large cytoplasmic domain that shows no obvious tyrosine kinase motif. In the present study, we report the establishment of a system in which the cDNA-directed human IL-2R beta allows growth signal transduction in a mouse pro-B cell line. This system enabled us to identify a unique region within the cytoplasmic domain of the human IL-2R beta chain essential for ligand-mediated signal transduction. We also demonstrate that certain cytoplasmic deletion mutants in the IL-2R beta chain, although deficient in signal transduction, can still form high affinity IL-2R in conjunction with endogenous mouse IL-2R alpha chain; the mutants are still able to internalize the ligand as well.

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