Alternate signalling pathways from the interleukin-2 receptor

Ellery, Jonathan M. and Nicholls, Peter J. (2002) Alternate signalling pathways from the interleukin-2 receptor. Cytokine & Growth Factor Reviews, 13 (1). pp. 27-40. ISSN 1359-6101. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1016/S1359-6101(01)00023-5

Abstract

Interleukin-2 (IL-2) plays a major role in the proliferation of cell populations during an immune reaction. The beta(c) and gamma(c) subunits of the IL-2 receptor (IL-2R) are sufficient and necessary for signal transduction. Despite lacking known catalytic domains, receptor engagement leads to the activation of a diverse array protein tyrosine kinases (PTKs). In resting or anergised T cells, Jak3 is not activated. Signals arising from the PROX domain of the gamma(c) subunit activate p56(lck) (lck) leading to the induction of anti-apoptotic mechanisms. When Jak3 is activated, in primed T cells, other PTKs predominantly mediate the induction of anti-apoptotic mechanisms and drive cellular proliferation. This review intends to suggest a role for these differences within the context of the immune system.

Item Type: Article
Additional information: 1359-6101 (Print) Journal Article Review
Uncontrolled keywords: interleukin-2 receptor (IL-2R); Jak3; phosphatidylinositol 3 kinase (PI3K) Dimerization Humans Interleukin-2/metabolism Janus Kinase 3 Mitogen-Activated Protein Kinase 1/metabolism Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases/metabolism Models, Biological Protein-Tyrosine Kinases/metabolism Receptors, Antigen, T-Cell/metabolism Receptors, Interleukin-2/*metabolism *Signal Transduction Transcription, Genetic
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Biomedical Research Group
Depositing User: Peter Nicholls
Date Deposited: 17 Sep 2008 12:12
Last Modified: 03 Jun 2014 08:40
Resource URI: https://kar.kent.ac.uk/id/eprint/7459 (The current URI for this page, for reference purposes)
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