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Titolo:
A strategy to make constitutively active MAP kinase by fusing with constitutively active MAP kinase kinase
Autore:
Miyata, Y; Adachi, S; Mizuno, H; Nishida, E;
Indirizzi:
Kyoto Univ, Grad Sch Sci, Dept Biophys, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 t Biophys, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ, Grad Sch Biostudies, Dept Cell & Dev Biol, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 Dev Biol, Sakyo Ku, Kyoto 6068502, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
fascicolo: 2-3, volume: 1451, anno: 1999,
pagine: 334 - 342
SICI:
0167-4889(19990921)1451:2-3<334:ASTMCA>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR EXPORT SIGNAL; PHOSPHORYLATION; TRANSFORMATION; INDUCTION; PATHWAYS; CASCADES; ACTIVATION; SUFFICIENT; MECHANISM; PROTEINS;
Keywords:
extracellular signal-regulated kinase; fusion protein; mitogen-activated protein kinase cascade; signal transduction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Nishida, E Kyoto Univ, Grad Sch Sci, Dept Biophys, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 Sakyo Ku, Kyoto 6068502, Japan
Citazione:
Y. Miyata et al., "A strategy to make constitutively active MAP kinase by fusing with constitutively active MAP kinase kinase", BBA-MOL CEL, 1451(2-3), 1999, pp. 334-342

Abstract

Classical mitogen-activated protein kinases (MAPKs) play a pivotal role ina variety of cellular signal transduction pathways. MAPKs are activated byphosphorylation at specific threonine and tyrosine residues catalyzed by upstream MAPK kinases (MAPKKs). Mutations of these two activation phosphorylation sites into acidic amino acids, however, do not convert MAPKs into constitutively active forms. Here, we report an approach to make a molecule with constitutive MAPK activity. The nuclear export signal-disrupted, constitutively active MAPKK was fused to the N-terminal end of wildtype MAPK. Whenthe resulting fusion protein was expressed in Escherichia coil, the MAPK moiety became phosphorylated and the fusion protein was constitutively active as MAPK. Moreover, when expressed in mammalian cultured cells, the fusionprotein was also activated as MAPK and was able to induce marked morphological changes in NIH-3T3 cells. These results suggest that the fusion protein can work as constitutively active MAPK and that this approach may be applicable to other members of the MAPK; family to make constitutively active forms. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 09:27:35