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(Received for publication, October 25, 1995, and in revised form, March 21, 1996)
From the Distinct yet overlapping sets of STAT
transcription factors are activated by different cytokines. One example
is the differential activation of acute phase response factor (APRF,
also called Stat3) and Stat1 by interleukin 6 and interferon-
Volume 271, Number 22,
Issue of May 31, 1996
pp. 12999-13007
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
II. Src HOMOLOGY SH2 DOMAINS DEFINE THE SPECIFICITY OF STAT
FACTOR ACTIVATION
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and
Institute of Biochemistry,
Rheinisch-Westfälische Technische Hochschule Aachen, 52057
Aachen, Germany and the § Laboratory of Molecular Cell
Biology, Rockefeller University, New York, New York 10021
.
Interleukin 6 activates both factors while, at least in human cells,
interferon- recruits only Stat1. Stat1 activation by interferon-
is mediated through a cytosolic tyrosine motif, Y440, of the
interferon- receptor. In an accompanying paper (Gerhartz, C.,
Heesel, B., Sasse, J., Hemmann, U., Landgraf, C., Schneider-Mergener,
J., Horn, F., Heinrich, P. C., and Graeve, L. (1996) J. Biol.
Chem. 271, 12991-12998), we demonstrated that two tyrosine
motifs within the cytoplasmic part of the interleukin 6 signal
transducer gp130 specifically mediate APRF activation while two others
can recruit both APRF and Stat1. By expressing a series of Stat1/APRF
domain swap mutants in COS-7 cells, we now determined which domains of
Stat1 and APRF are involved in the specific recognition of
phosphotyrosine motifs. Our data demonstrate that the SH2 domain is the
sole determinant of specific STAT factor recruitment. Furthermore, the
SH2 domain of Stat1 is able to recognize two unrelated types of
phosphotyrosine motifs, one represented by the interferon- receptor
Y440DKPH peptide, and the other by two gp130 YXPQ motifs.
By molecular modeling, we propose three-dimensional model structures of
the Stat1 and APRF SH2 domains which allow us to explain the different
binding preferences of these factors and to predict amino acids crucial
for specific peptide recognition.
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