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Titolo:
Cdc42p functions at the docking stage of yeast vacuole membrane fusion
Autore:
Muller, O; Johnson, DI; Mayer, A;
Indirizzi:
Max Planck Gesell, Friedrich Miescher Lab, D-72076 Tubingen, Germany Max Planck Gesell Tubingen Germany D-72076 ab, D-72076 Tubingen, Germany Univ Vermont, Markey Ctr Mol Genet, Dept Microbiol & Mol Genet, Burlington, VT 05405 USA Univ Vermont Burlington VT USA 05405 Mol Genet, Burlington, VT 05405 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 20, volume: 20, anno: 2001,
pagine: 5657 - 5665
SICI:
0261-4189(20011015)20:20<5657:CFATDS>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALDRICH-SYNDROME PROTEIN; SACCHAROMYCES-CEREVISIAE GENE; GTPASE-BINDING DOMAIN; CIS-SNARE COMPLEX; CELL POLARITY; ARP2/3 COMPLEX; BUDDING YEAST; T-SNARE; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; VESICULAR TRANSPORT;
Keywords:
actin; Rho GTPase; Saccharomyces cerevisiae; SNARE; tethering;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
89
Recensione:
Indirizzi per estratti:
Indirizzo: Mayer, A Max Planck Gesell, Friedrich Miescher Lab, Spemannstr 37-39, D-72076 Tubingen, Germany Max Planck Gesell Spemannstr 37-39 Tubingen Germany D-72076 many
Citazione:
O. Muller et al., "Cdc42p functions at the docking stage of yeast vacuole membrane fusion", EMBO J, 20(20), 2001, pp. 5657-5665

Abstract

Membrane fusion reactions have been considered to be primarily regulated by Rab GTPases. In the model system of homotypic vacuole fusion in the yeastSaccharomyces cerevisiae, we show that Cdc42p, a member of the Rho family of GTPases, has a direct role in membrane fusion. Genetic evidence suggested a relationship between Cdc42p and Vtc1p/Nrf1p, a central part of the vacuolar membrane fusion machinery. Vacuoles from cdc42 temperature-sensitive mutants are deficient for fusion at the restrictive temperature. Specific amino acid changes on the Cdc42p protein surface in these mutants define the putative interaction domain that is crucial for its function in membrane fusion. Affinity-purified antibodies to this domain inhibited the in vitro fusion reaction. Using these antibodies in kinetic analyses and assays for subreactions of the priming, docking and post-docking phase of the reaction, we show that Cdc42p action follows Ypt7p-dependent tethering, but precedes the formation of trans-SNARE complexes. Thus, our data define an effector binding domain of Cdc42p by which it regulates the docking reaction of vacuole fusion.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 10:00:47