Functional cleavage of the common cytokine receptor γ chain (γc) by calpain

Noguchi, Masayuki ; Sarin, Apurva ; Javad Aman, M. ; Nakajima, Hiroshi ; Shores, Elizabeth W. ; Henkart, Pierre A. ; Leonard, Warren J. (1997) Functional cleavage of the common cytokine receptor γ chain (γc) by calpain PNAS, 94 (21). pp. 11534-11539. ISSN 0027-8424

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The small subunit of calpain, a calcium-dependent cysteine protease, was found to interact with the cytoplasmic domain of the common cytokine receptor γ chain (γ c) in a yeast two-hybrid interaction trap assay. This interaction was functional as demonstrated by the ability of calpain to cleave in vitro-translated wild-type γc, but not γc containing a mutation in the PEST (proline, glutamate, serine, and threonine) sequence in its cytoplasmic domain, as well as by the ability of endogenous calpain to mediate cleavage of γc in a calcium-dependent fashion. In T cell receptor-stimulated murine thymocytes, calpain inhibitors decreased cleavage of γ c. Moreover, in single positive CD4+ thymocytes, not only did a calpain inhibitor augment CD3-induced proliferation, but antibodies to γ c blocked this effect. Finally, treatment of cells with ionomycin could inhibit interleukin 2-induced STAT protein activation, but this inhibition could be reversed by calpain inhibitors. Together, these data suggest that calpain-mediated cleavage of γc represents a mechanism by which γc-dependent signaling can be controlled.

Item Type:Article
Source:Copyright of this article belongs to National Academy of Sciences.
ID Code:62168
Deposited On:19 Sep 2011 11:47
Last Modified:19 Sep 2011 11:47

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