Publication Date:
1994-04-01
Description:
The STAT family of proteins carries out a dual function: signal transduction and activation of transcription. A new family member, Stat3, becomes activated through phosphorylation on tyrosine as a DNA binding protein in response to epidermal growth factor (EGF) and interleukin-6 (IL-6) but not interferon gamma (IFN-gamma). It is likely that this phosphoprotein forms homodimers as well as heterodimers with the first described member of the STAT family, Stat91 (renamed Stat1 alpha), which is activated by the IFNs and EGF. Differential activation of different STAT proteins in response to different ligands should help to explain specificity in nuclear signaling from the cell surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhong, Z -- Wen, Z -- Darnell, J E Jr -- AI32489/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):95-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140422" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Base Sequence
;
Cell Line
;
DNA/metabolism
;
DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism
;
Epidermal Growth Factor/*pharmacology
;
Humans
;
Interferon-gamma
;
Interleukin-6/*pharmacology
;
Mice
;
Molecular Sequence Data
;
Phosphorylation
;
Regulatory Sequences, Nucleic Acid
;
STAT1 Transcription Factor
;
STAT3 Transcription Factor
;
Sequence Alignment
;
Trans-Activators/metabolism
;
Transfection
;
Tumor Cells, Cultured
;
Tyrosine/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
