Receptor to nucleus signaling via tyrosine phosphorylation of the p91 transcription factor

Christopher Daly; Nancy C. Reich

doi:10.1016/1043-2760(94)90013-2

Receptor to nucleus signaling via tyrosine phosphorylation of the p91 transcription factor

Christopher Daly
, Nancy C. Reich

Microbiology and Immunology

Stony Brook University

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

Recent studies on signal transduction stimulated by interferons have defined pathways that link cell surface receptors to target genes in the nucleus. After interferon binding, nonreceptor tyrosine kinases are activated that phosphorylate components of latent DNA-binding factors in the cytoplasm. These phosphorylated factors form multimeric complexes that translocate to the nucleus and bind to specific DNA sequences in the promoters of induced genes. A 91-kD factor (p91 or Stat 91) is activated by interferons and serves as a subunit partner in the composition of diverse transcription factors.

Original language	English
Pages (from-to)	159-164
Number of pages	6
Journal	Trends in Endocrinology and Metabolism
Volume	5
Issue number	4
DOIs	https://doi.org/10.1016/1043-2760(94)90013-2
State	Published - 1994

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10.1016/1043-2760(94)90013-2

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title = "Receptor to nucleus signaling via tyrosine phosphorylation of the p91 transcription factor",

abstract = "Recent studies on signal transduction stimulated by interferons have defined pathways that link cell surface receptors to target genes in the nucleus. After interferon binding, nonreceptor tyrosine kinases are activated that phosphorylate components of latent DNA-binding factors in the cytoplasm. These phosphorylated factors form multimeric complexes that translocate to the nucleus and bind to specific DNA sequences in the promoters of induced genes. A 91-kD factor (p91 or Stat 91) is activated by interferons and serves as a subunit partner in the composition of diverse transcription factors.",

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AU - Daly, Christopher

AU - Reich, Nancy C.

PY - 1994

Y1 - 1994

N2 - Recent studies on signal transduction stimulated by interferons have defined pathways that link cell surface receptors to target genes in the nucleus. After interferon binding, nonreceptor tyrosine kinases are activated that phosphorylate components of latent DNA-binding factors in the cytoplasm. These phosphorylated factors form multimeric complexes that translocate to the nucleus and bind to specific DNA sequences in the promoters of induced genes. A 91-kD factor (p91 or Stat 91) is activated by interferons and serves as a subunit partner in the composition of diverse transcription factors.

AB - Recent studies on signal transduction stimulated by interferons have defined pathways that link cell surface receptors to target genes in the nucleus. After interferon binding, nonreceptor tyrosine kinases are activated that phosphorylate components of latent DNA-binding factors in the cytoplasm. These phosphorylated factors form multimeric complexes that translocate to the nucleus and bind to specific DNA sequences in the promoters of induced genes. A 91-kD factor (p91 or Stat 91) is activated by interferons and serves as a subunit partner in the composition of diverse transcription factors.

UR - https://www.scopus.com/pages/publications/0028362313

U2 - 10.1016/1043-2760(94)90013-2

DO - 10.1016/1043-2760(94)90013-2

M3 - Article

AN - SCOPUS:0028362313

SN - 1043-2760

VL - 5

SP - 159

EP - 164

JO - Trends in Endocrinology and Metabolism

JF - Trends in Endocrinology and Metabolism

IS - 4

ER -

Receptor to nucleus signaling via tyrosine phosphorylation of the p91 transcription factor

Abstract

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