Publication Date:
1996-09-20
Description:
STAT proteins (signal transducers and activators of transcription) are latent cytoplasmic transcription factors that are phosphorylated by Janus kinases in response to cytokines. Phosphorylated STAT proteins translocate to the nucleus, where they transiently turn on specific sets of cytokine-inducible genes. The mechanism that controls the amounts of activated STAT proteins is not understood. STAT1 proteins activated by interferon-gamma treatment in HeLa cells were shown to be stabilized by a proteasome inhibitor and ubiquitinated in vivo. Thus, the amount of activated STAT1 may be negatively regulated by the ubiquitin-proteasome pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, T K -- Maniatis, T -- AI20642/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1717-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8781235" target="_blank"〉PubMed〈/a〉
Keywords:
Cell Nucleus/metabolism
;
Cysteine Endopeptidases/*metabolism
;
Cysteine Proteinase Inhibitors/pharmacology
;
DNA/metabolism
;
DNA-Binding Proteins/*metabolism
;
HeLa Cells
;
Humans
;
Immunoblotting
;
Interferon-gamma/*pharmacology
;
Leupeptins/pharmacology
;
Multienzyme Complexes/*metabolism
;
Mutation
;
Phosphorylation
;
Proteasome Endopeptidase Complex
;
STAT1 Transcription Factor
;
Signal Transduction
;
Trans-Activators/*metabolism
;
Tumor Cells, Cultured
;
Ubiquitins/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics