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(Received for publication, August 6, 1996)
From the Recent work has shown that IL-10 induces
activation of the JAK-STAT signaling pathway. To define the mechanism
underlying signal transducer and activator of transcription (STAT)
protein recruitment to the interleukin 10 (IL-10) receptor, the STAT
proteins activated by IL-10 in different cell populations were first
defined using electrophoretic mobility shift assays. In all cells
tested, IL-10 activated Stat1 and Stat3 and induced the formation of
three distinct DNA binding complexes that contained different
combinations of these two transcription factors. IL-10 also activated
Stat5 in Ba/F3 cells that stably expressed the murine IL-10 receptor.
Using a structure-function mutagenesis approach, two tyrosine residues
(Tyr427 and Tyr477) in the intracellular domain
of the murine IL-10 receptor were found to be redundantly required for
receptor function and for activation of Stat3 but not for Stat1 or
Stat5. Twelve amino acid peptides encompassing either of these two
tyrosine residues in phosphorylated form coprecipitated Stat3 but not
Stat1 and blocked IL-10-induced Stat3 phosphorylation in a cell-free
system. In contrast, tyrosine-phosphorylated peptides containing
Tyr374 or Tyr396 did not interact with Stat3 or
block Stat3 activation. These data demonstrate that Stat3 but not Stat1
or Stat5 is directly recruited to the ligand-activated IL-10 receptor
by binding to specific but redundant receptor intracellular domain
sequences containing phosphotyrosine. This study thus supports the
concept that utilization of distinct STAT proteins by different
cytokine receptors is dependent on the expression of particular
ligand-activatable, tyrosine-containing STAT docking sites in receptor
intracellular domains.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27954-27961
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
Center for Immunology, Department of
Pathology, Washington University School of Medicine, St. Louis,
Missouri 63110, 
Department of Molecular Biology, DNAX Research
Institute, Palo Alto, California 94304, and '' Laboratory of Molecular
Cell Biology, Rockefeller University, New York, New York 10021
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