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Regulation of Golgi structure through heterotrimeric G proteins.
Jamora, C; Takizawa, P A; Zaarour, R F; Denesvre, C; Faulkner, D J; Malhotra, V.
Afiliación
  • Jamora C; Department of Biology, University of California San Diego, La Jolla 92093-0347, USA.
Cell ; 91(5): 617-26, 1997 Nov 28.
Article en En | MEDLINE | ID: mdl-9393855
ABSTRACT
We have previously shown that ilimaquinone (IQ), a marine sponge metabolite, causes complete vesiculation of the Golgi stacks. By reconstituting the IQ-mediated vesiculation of the Golgi apparatus in permeabilized cells, we now demonstrate that this process does not require ARF and coatomers, which are necessary for the formation of Golgi-derived COPI vesicles. We find that IQ-mediated Golgi vesiculation is inhibited by G alpha(s)-GDP and G alpha(i3)-GDP. Interestingly, adding betagamma subunits in the absence of IQ is sufficient to vesiculate Golgi stacks. Our findings reveal that IQ-mediated Golgi vesiculation occurs through activation of heterotrimeric G proteins and that it is the free betagamma, and not the activated alpha subunit, that triggers Golgi vesiculation.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión al GTP / Aparato de Golgi Límite: Animals Idioma: En Revista: Cell Año: 1997 Tipo del documento: Article País de afiliación: Estados Unidos
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión al GTP / Aparato de Golgi Límite: Animals Idioma: En Revista: Cell Año: 1997 Tipo del documento: Article País de afiliación: Estados Unidos