Ellery, Jonathan M. and Kempshall, Sarah J. and Nicholls, Peter J. (2000) Activation of the interleukin 2 receptor: a possible role for tyrosine phosphatases. Cellular Signalling, 12 (6). pp. 367-373. ISSN 0898-6568. (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)
Engagement of interleukin-2 (IL-2) mediates the heterodimeridation of the common beta chain (beta(c)) and common gamma chain (gamma(c)) of the IL-2 receptor (IL-2R). This is sufficient and necessary for receptor activation and signal transduction. It is generally held that the IL-2R is activated by the trans-activity of the protein tyrosine kinases (PTKs) Jak1 and Jak3 associated with beta(c) and gamma(c) respectively. Transduction of proliferative signals requires Jak3 activity. A Jak3 independent signalling pathway involving p56(lck), generating anti-apoptotic signals, can be observed and requires the PROX domain of gamma(c). p56(lck) can be activated by dephosphorylation of an inhibitory carboxyl terminal phosphorylated tyrosine residue (Y505). We propose that this is mediated by a PROX domain associated protein tyrosine phosphatase (PTP). Activation of p56(lck) alone is insufficient for transduction of proliferative signals and thus works in concert with Jak3 mediated receptor activation. This indicates that both gamma(c) domains are vital for signal transduction.
|Uncontrolled keywords:||interleukin-2; IL-2R; phosphatase; lck; Jak3; dephosphorylation|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||O.O. Odanye|
|Date Deposited:||19 May 2009 01:58|
|Last Modified:||03 Jun 2014 08:41|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/16063 (The current URI for this page, for reference purposes)|