A Stat3-Interacting Protein (StIP1) Regulates Cytokine Signal Transduction

Genetic and biochemical studies have led to the identification of the Stat3-Interacting Protein StIP1. The preferential association of StIP1 with inactive (i.e., unphosphorylated) Stat3 suggests that it may contribute to the regulation of Stat3 activation. Consistent with this possibility, StIP1 als...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2000-08, Vol.97 (18), p.10120-10125
Main Authors: Collum, R G, Brutsaert, S, Lee, G, Schindler, C
Format: Article
Language:English
Subjects:
3T3 Cells
Amino Acid Sequence
Amino acids
Animals
Antibodies
Biochemistry
Biological Sciences
Biotechnology
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell Line
Complementary DNA
Cytokines
Cytokines - physiology
DNA-Binding Proteins - metabolism
Gene expression regulation
Genetics
Hep G2 cells
Humans
Immunology
Intracellular Signaling Peptides and Proteins
Mice
Molecular Sequence Data
Protein Biosynthesis
Protein-Tyrosine Kinases - metabolism
Proteins
Recombinant Proteins - metabolism
Scaffolds
Sequence Alignment
Sequence Homology, Amino Acid
Signal Transduction - physiology
Stat3 protein
STAT3 Transcription Factor
Stat3-interacting protein
StIP1 protein
Trans-Activators - metabolism
Transcription, Genetic
Transfection
Tumor Cells, Cultured
Yeasts
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Summary:Genetic and biochemical studies have led to the identification of the Stat3-Interacting Protein StIP1. The preferential association of StIP1 with inactive (i.e., unphosphorylated) Stat3 suggests that it may contribute to the regulation of Stat3 activation. Consistent with this possibility, StIP1 also exhibits an affinity for members of the Janus kinase family. Overexpression of the Stat3-binding domain of StIP1 blocks Stat3 activation, nuclear translocation, and Stat3-dependent induction of a reporter gene. These studies indicate that StIP1 regulates the ligand-dependent activation of Stat3, potentially by serving as a scaffold protein that promotes the interaction between Janus kinases and their Stat3 substrate. The ability of StIP1 to associate with several additional members of the signal transducer and activator of transcription family suggests that StIP1 may serve a broader role in cytokine-signaling events.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.170192197