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Titolo:
Unexpected effects of FERM domain mutations on catalytic activity of Jak3:Structural implication for Janus kinases
Autore:
Zhou, YJ; Chen, M; Cusack, NA; Kimmel, LH; Magnuson, KS; Boyd, JG; Lin, W; Roberts, JL; Lengi, A; Buckley, RH; Geahlen, RL; Candotti, F; Gadina, M; Changelian, PS; OShea, JJ;
Indirizzi:
NIAMSD, Lymphocyte Cell Biol Sect, Arthrit & Rheumatism Branch, NIH, Bethesda, MD 20892 USA NIAMSD Bethesda MD USA 20892 eumatism Branch, NIH, Bethesda, MD 20892 USA NHGRI, Genet & Mol Biol Branch, NIH, Bethesda, MD 20892 USA NHGRI Bethesda MD USA 20892 Mol Biol Branch, NIH, Bethesda, MD 20892 USA Pfizer Inc, Global Res & Dev, Dept Immunol, Groton, CT 06340 USA Pfizer Inc Groton CT USA 06340 & Dev, Dept Immunol, Groton, CT 06340 USA Duke Univ, Sch Med, Dept Pediat, Durham, NC 27710 USA Duke Univ Durham NCUSA 27710 Sch Med, Dept Pediat, Durham, NC 27710 USA Purdue Univ, Dept Med Chem & Mol Pharmacol, W Lafayette, IN 47907 USA Purdue Univ W Lafayette IN USA 47907 Pharmacol, W Lafayette, IN 47907 USA
Titolo Testata:
MOLECULAR CELL
fascicolo: 5, volume: 8, anno: 2001,
pagine: 959 - 969
SICI:
1097-2765(200111)8:5<959:UEOFDM>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASES; MICE LACKING JAK3; PSEUDOKINASE DOMAIN; BINDING-SITE; ACTIVATION; SRC; PHOSPHORYLATION; INHIBITORS; TERMINUS; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: O'Shea, JJ NIAMSD, Lymphocyte Cell Biol Sect, Arthrit & Rheumatism Branch,NIH, Bethesda, MD 20892 USA NIAMSD Bethesda MD USA 20892 anch, NIH, Bethesda, MD 20892 USA
Citazione:
Y.J. Zhou et al., "Unexpected effects of FERM domain mutations on catalytic activity of Jak3:Structural implication for Janus kinases", MOL CELL, 8(5), 2001, pp. 959-969

Abstract

Janus kinases comprise carboxyterminal kinase, pseudokinase, SH2-like, andN-terminal FERM domains. We identified three patient-derived mutations in the FERM domain of Jak3 and investigated the functional consequences of these mutations. These mutations inhibited receptor binding and also abrogatedkinase activity, suggesting interactions between the FERM and kinase domains. In fact, the domains were found to physically associate, and coexpression of the FERM domain enhanced activity of the isolated kinase domain. Conversely, staurosporine, which alters kinase domain structure, disrupted receptor binding, even though the catalytic activity of Jak3 is dispensable forreceptor binding. Thus, the Jak FERM domain appears to have two critical functions: receptor interaction and maintenance of kinase integrity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 17:08:11