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Titolo:
STAT3 SERINE PHOSPHORYLATION BY ERK-DEPENDENT AND ERK-INDEPENDENT PATHWAYS NEGATIVELY MODULATES ITS TYROSINE PHOSPHORYLATION
Autore:
CHUNG JK; UCHIDA E; GRAMMER TC; BLENIS J;
Indirizzi:
HARVARD UNIV,SCH MED,DEPT CELL BIOL,240 LONGWOOD AVE BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT CELL BIOL BOSTON MA 02115
Titolo Testata:
Molecular and cellular biology
fascicolo: 11, volume: 17, anno: 1997,
pagine: 6508 - 6516
SICI:
0270-7306(1997)17:11<6508:SSPBEA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMAL GROWTH-FACTOR; SIGNAL-TRANSDUCTION PATHWAY; DNA-BINDING ACTIVITY; PROTEIN-KINASES; INTERFERON ACTIVATION; TARGETED DISRUPTION; CYTOKINE RECEPTORS; GENE-EXPRESSION; TRANSCRIPTION; INTERLEUKIN-6;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
J.K. Chung et al., "STAT3 SERINE PHOSPHORYLATION BY ERK-DEPENDENT AND ERK-INDEPENDENT PATHWAYS NEGATIVELY MODULATES ITS TYROSINE PHOSPHORYLATION", Molecular and cellular biology, 17(11), 1997, pp. 6508-6516

Abstract

Recent studies have indicated that serine phosphorylation regulates the activities of STAT1 and STAT3. However, the kinase(s) responsible and the role of serine phosphorylation in STAT function remain unresolved. In the present studies, we examined the growth factor-dependent serine phosphorylation of STAT1 and STAT3, We provide in vitro and in vivo evidence that the ERK family of mitogen-activated protein (MAP) kinases, but not JNK or p38, specifically phosphorylate STAT3 at serine 727 in response to growth factors. Evidence for additional mitogen-regulated serine phosphorylation is also provided, STAT1 is a relatively poor substrate for all MAP kinases tested both in vitro and in vivo. STAT3 serine phosphorylation, not its tyrosine phosphorylation, results in retarded mobility of the STAT3 protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Importantly, serine 727 phosphorylation negatively modulates STAT3 tyrosine phosphorylation, which is required for dimer formation, nuclear translocation, and the DNA binding activity of this transcriptional regulator. Interestingly, the cytokineinterleukin-6 also stimulates STAT3 serine phosphorylation, but in contrast to growth factors, this occurs by an ERK-independent process.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 07:06:04