Internalization and nuclear localization of interleukin 1 are not sufficient for function.

A. Heguy, C. Baldari, K. Bush, R. Nagele, R. C. Newton, R. J. Robb, R. Horuk, J. L. Telford, M. Melli

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

The human fibroblast interleukin 1 (IL-1) receptor is a glycosylated transmembrane protein with a cytoplasmic domain of 213 amino acids. We have constructed a series of deletion mutants of the cytoplasmic region of the IL 1 receptor and have used these mutants to examine its role in ligand binding, internalization, signal transduction, and nuclear localization of IL-1. Mutant receptors lacking most of the cytoplasmic domain are expressed at the cell surface and can bind, internalize, and localize IL-1 at the nucleus, but they do not allow IL-1-mediated induction of interleukin 2 and SV40 promoters. We have localized a critical region for signal transduction to a 50-amino acid segment of the cytoplasmic domain of the receptor. These studies demonstrate that IL-1 internalization and nuclear localization are not sufficient to trigger IL-1 activation of gene expression in T-cells.

Original languageEnglish (US)
Pages (from-to)311-315
Number of pages5
JournalCell growth & differentiation : the molecular biology journal of the American Association for Cancer Research
Volume2
Issue number7
StatePublished - Jul 1991

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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