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INTERFERON ACTIVATION OF THE TRANSCRIPTION FACTOR STAT91 INVOLVES DIMERIZATION THROUGH SH2-PHOSPHOTYROSYL PEPTIDE INTERACTIONS
被引:716
作者:
SHUAI, K
[1
]
HORVATH, CM
[1
]
HUANG, LHT
[1
]
QURESHI, SA
[1
]
COWBURN, D
[1
]
DARNELL, JE
[1
]
机构:
[1] ROCKEFELLER UNIV, PLANT BIOCHEM LAB, NEW YORK, NY 10021 USA
来源:
关键词:
D O I:
10.1016/0092-8674(94)90357-3
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Stat91 (a 91 kd protein that acts as a signal transducer and activator of transcription) is inactive in the cytoplasm of untreated cells but is activated by phosphorylation on tyrosine in response to a number of polypeptide ligands, including interferon alpha (IFN-alpha) and lFN-gamma. We report here that the inactive Stat91 in the cytoplasm of untreated cells is a monomer and that upon IFN-gamma-induced phosphorylation it forms a stable homodimer. Only the dimer is capable of binding to a specific DNA sequence directing transcription. Through dissociation and reassociation assays, we show that dimerization of Stat91 is mediated through SH2-phosphotyrosyl peptide interactions. Dimerization involving SH2 recognition of specific phosphotyrosyl peptides may well provide a prototype for interactions among family members of STAT proteins to form different transcription complexes.
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页码:821 / 828
页数:8
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