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Titolo:
Rho-dependence of Schizosaccharomyces pombe Pck2
Autore:
Sayers, LG; Katayama, S; Nakano, K; Mellor, H; Mabuchi, I; Toda, T; Parker, PJ;
Indirizzi:
Imperial Canc Res Fund, Prot Phosphorylat Lab, London WC2A 3PX, England Imperial Canc Res Fund London England WC2A 3PX London WC2A 3PX, England Imperial Canc Res Fund, Cell Regulat Lab, London WC2A 3PX, England Imperial Canc Res Fund London England WC2A 3PX London WC2A 3PX, England Univ Tokyo, Sch Arts & Sci, Div Biol, Tokyo 1538902, Japan Univ Tokyo Tokyo Japan 1538902 rts & Sci, Div Biol, Tokyo 1538902, Japan Natl Inst Basic Biol, Dept Cell Biol, Okazaki, Aichi 4448585, Japan Natl Inst Basic Biol Okazaki Aichi Japan 4448585 ki, Aichi 4448585, Japan
Titolo Testata:
GENES TO CELLS
fascicolo: 1, volume: 5, anno: 2000,
pagine: 17 - 27
SICI:
1356-9597(200001)5:1<17:ROSPP>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; GTP-BINDING PROTEIN; CELL-SHAPE CONTROL; FISSION YEAST; SACCHAROMYCES-CEREVISIAE; ACTIVATION; TARGET; GENE; LOCALIZATION; ORGANIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Parker, PJ Imperial Canc Res Fund, Prot Phosphorylat Lab, 44 Lincolns Inn Fields, London WC2A 3PX, England Imperial Canc Res Fund 44 Lincolns Inn Fields London England WC2A 3PX
Citazione:
L.G. Sayers et al., "Rho-dependence of Schizosaccharomyces pombe Pck2", GENES CELLS, 5(1), 2000, pp. 17-27

Abstract

Background: In metazoans, the HR1 domain, a motif found in a number of proteins including the protein kinase C-related PRKs, is responsible for an interaction with Rho-GTPases. The structural similarity between the Schizosaccaromyces pombe Pck proteins and the mammalian Rho-dependent protein kinaseC-related family, has led us to investigate the relationship between the function of Rho and that of Pck1/2. Results: Rho1 is shown to interact with the conserved N-terminal HR1 domain of Pck1/2 in vitro and in vivo. Lethal overproduction of Rho1 is neutralized by co-expression of the Pck2 HR1 domain, which by itself compromises growth when overproduced. The Pck2-Rho1 interaction has a profound effect on the steady state expression of Pck2 and this is shown to parallel the immunoprecipitated activity and phosphorylation of Pck2 at its activation loop site. It is further shown that Pck2 becomes localized at the septum, where Rho1 is also located. Conclusions: The results demonstrate that the Pck proteins are Rho1 effectors in fission yeast and that the HR1 domain is a universal motif for the Rho-GTPase interaction. Furthermore, the evidence supports the contention that the yeast Pck1 and Pck2 proteins are primitive protein kinases, which invertebrates have evolved into the two distinct PKC and PRK families.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 08:51:18