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Titolo:
Arginine/lysine-rich structural element is involved in interferon-induced nuclear import of STATs
Autore:
Melen, K; Kinnunen, L; Julkunen, I;
Indirizzi:
Natl Publ Hlth Inst, Dept Microbiol, Lab Viral & Mol Immunol, FIN-00300 Helsinki, Finland Natl Publ Hlth Inst Helsinki Finland FIN-00300 N-00300 Helsinki, Finland Natl Publ Hlth Inst, Dept Epidemiol & Hlth Promot, Diabet & Genet Epidemiol Unit, FIN-00300 Helsinki, Finland Natl Publ Hlth Inst Helsinki Finland FIN-00300 N-00300 Helsinki, Finland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 19, volume: 276, anno: 2001,
pagine: 16447 - 16455
SICI:
0021-9258(20010511)276:19<16447:ASEIII>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; HUMAN MXB PROTEIN; DNA-BINDING; TRANSCRIPTION FACTOR; SIGNAL-TRANSDUCTION; GENE-EXPRESSION; ALPHA; TRANSLOCATION; LOCALIZATION; ACTIVATOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Melen, K Natl Publ Hlth Inst, Dept Microbiol, Lab Viral & Mol Immunol, Mannerheimintie 166, FIN-00300 Helsinki, Finland Natl Publ Hlth Inst Mannerheimintie 166 Helsinki Finland FIN-00300
Citazione:
K. Melen et al., "Arginine/lysine-rich structural element is involved in interferon-induced nuclear import of STATs", J BIOL CHEM, 276(19), 2001, pp. 16447-16455

Abstract

Signal transducers and activators of transcription (STATs) are latent cytoplasmic transcription factors, which mediate interferon (IFN), interleukin,and some growth factor and peptide hormone signaling in cells, IFN stimulation results in tyrosine phosphorylation, dimerization, and nuclear import of STATs. In response to IFN-gamma stimulation, STAT1 forms homodimers, whereas IFN-alpha induction results in the formation of STAT1.STAT2 heterodimers, which assemble with p48 protein in the nucleus. Phosphorylation as suchis not sufficient to target STATs into the nucleus; rather, the dimerization triggered by phosphorylation is essential. Although IFN-induced nuclear import of STATs is mediated by the importin/Ran transport system, no classic nuclear localization signal (NLS) has been found in STATs. In the three-dimensional structure of STAT1, we observed a structural arginine/lysine-rich element within the DNA-binding domain of the molecule. We created a series of point mutations in these elements of STAT1 and STAT2 and showed by transient transfection/IFN stimulation assay that this site is essential for the nuclear import of both STAT1 and STAT2. The results suggest that two arginine/lysine-rich elements, one in each STAT monomer, are required for IFN-induced nuclear import of STAT dimers, import-defective STAT1 and STAT2 proteins were readily phosphorylated and dimerized, but they functioned as dominant negative molecules inhibiting the nuclear import of heterologous STATprotein.

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Documento generato il 18/09/20 alle ore 16:14:27