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Blood, 15 September 2001, Vol. 98, No. 6, pp. 1935-1941
NEOPLASIA
The deubiquitinating enzyme DUB-2 prolongs cytokine-induced
signal transducers and activators of transcription activation and
suppresses apoptosis following cytokine withdrawal
Thi-Sau Migone,
Martine Humbert,
Anne Rascle,
David Sanden,
Alan D'Andrea, and
James A. Johnston
From the DNAX Research Institute of Molecular and
Cellular Biology, Palo Alto, CA, and the Division of Pediatric Oncology
and Cellular and Molecular Biology, Dana Farber Cancer Institute,
Harvard Medical School, Boston, MA.
Cytokines, such as interleukin-2 (IL-2), activate intracellular
signaling pathways via rapid tyrosine phosphorylation of their receptors, resulting in the activation of many genes involved in cell
growth and survival. The deubiquitinating enzyme DUB-2 is induced in
response to IL-2 but as yet its function has not been determined. The
results of this study show that DUB-2 is expressed in human T-cell
lymphotropic virus-I(HTLV-1)-transformed T cells that exhibit
constitutive activation of the IL-2 JAK/STAT (signal transducers and
activators of transcription) pathway, and when expressed in Ba/F3 cells
DUB-2 markedly prolonged IL-2-induced STAT5 phosphorylation. Although
DUB-2 did not enhance IL-2-mediated proliferation, when withdrawn from
growth factor, cells expressing DUB-2 had sustained STAT5
phosphorylation and enhanced expression of IL-2-induced genes
cis and c-myc. Moreover,
DUB-2 expression markedly inhibited apoptosis induced by cytokine
withdrawal allowing cells to survive. Taken together these data suggest
that DUB-2 can enhance signaling through the JAK/STAT pathway, prolong
lymphocyte survival, and, when constitutively expressed, may contribute
to the activation of the JAK/STAT pathway observed in some transformed cells.
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