Biomolecular interaction analysis of IFN gamma-induced signaling events in whole-cell lysates: Prevalence of latent STAT1 in high-molecular weight complexes

Lackmann, M., Harpur, A.G., Oates, A.C., Mann, R.J., Gabriel, A., Meutermans, W., Alewood, P.F., Kerr, I.M., Stark, G.R. and Wilks, A.F. (1998) Biomolecular interaction analysis of IFN gamma-induced signaling events in whole-cell lysates: Prevalence of latent STAT1 in high-molecular weight complexes. Growth Factors, 16 1: 39-51.

Author Lackmann, M.
Harpur, A.G.
Oates, A.C.
Mann, R.J.
Gabriel, A.
Meutermans, W.
Alewood, P.F.
Kerr, I.M.
Stark, G.R.
Wilks, A.F.
Title Biomolecular interaction analysis of IFN gamma-induced signaling events in whole-cell lysates: Prevalence of latent STAT1 in high-molecular weight complexes
Journal name Growth Factors   Check publisher's open access policy
ISSN 0897-7194
Publication date 1998
Sub-type Article (original research)
Volume 16
Issue 1
Start page 39
End page 51
Total pages 13
Place of publication United Kingdom
Publisher Informa Healthcare
Language eng
Abstract The basic framework for the JAK/STAT pathway is well documented. Recruitment of latent cytoplasmic STAT transcription factors to tyrosine phosphorylated docking sites on cytokine receptors and their JAK-mediated phosphorylation instigates their translocation to the nucleus and their ability to bind DNA, The biochemical processes underlying recruitment and activation of this pathway have commonly been studied in reconstituted in vitro systems using previously defined recombinant signaling components. We have dissected the Interferon gamma (IFN gamma) signal transduction pathway in crude extracts from wild-type and STAT1-negative mutant cell Lines by real-time BIAcore analysis, size-exclusion (SE) chromatography and immune-detection. The data indicate that in detergent-free cell extracts: (1) the phospho-tyrosine (Y440P)-containing peptide motif of the IFN gamma-receptor ct-chain interacts directly with STAT1, or STAT1 complexes, and no other protein; (2) nonactivated STAT 1 is present in a higher molecular weight complex(es) and, at least for IFN gamma-primed cells, is available for recruitment to the activated IFN gamma-receptor from only a subset of such complexes; (3) activated STAT1 is released from the receptor as a monomer.
Keyword Cell Biology
Endocrinology & Metabolism
Jak/stat Pathway
Sh2 Domain
Phospho-tyrosine
Bia
Colony-stimulating Factor
Tyrosine Kinase Jak1
Interferon-gamma
Transcription Factor
Alpha Interferon
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Mon, 13 Aug 2007, 10:42:14 EST