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(Received for publication, September 10, 1996)
From the To gain insight into the intracellular signaling
cascades that are activated by the binding of interleukin-3 (IL-3) to
its target cells, we have embarked on the identification of proteins that are associated with the IL-3 receptor (IL-3R). In a previous study
we reported that a 110-kDa serine/threonine protein kinase is
constitutively associated with the IL-3R and activated following IL-3
stimulation. We now report that a
phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3) 5-phosphatase (5-ptase) is also
constitutively associated with the IL-3R. This 5-ptase is
magnesium-dependent and removes the 5-position phosphate
from PtdIns-3,4,5-P3 but does not metabolize
PtdIns-4,5-P2, inositol (Ins)-1,3,4,5-P4, or
Ins-1,4,5-P3. This substrate specificity distinguishes it
from any previously characterized 5-ptase. Interestingly, it may be bound indirectly via phosphatidylinositol 3-kinase (PI 3-kinase), another enzyme that is constitutively bound to the IL-3R. However, unlike PI 3-kinase which becomes activated following IL-3 stimulation, this receptor-associated 5-ptase activity does not increase following IL-3 stimulation, and its primary function may be to keep the principal in vivo product of PI 3-kinase,
PtdIns-3,4,5-P3, at low levels in unstimulated cells,
to terminate the PI 3-kinase signal following IL-3 stimulation or to
metabolize PtdIns-3,4,5-P3 to a metabolically active second
messenger, i.e. PtdIns-3,4-P2.
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29729-29733
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Terry Fox Laboratory, British Columbia
Cancer Agency, University of British Columbia, Vancouver, British
Columbia, Canada V5Z 1L3 and § Washington University School
of Medicine, St Louis, Missouri 63110
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