The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8.
Proc Natl Acad Sci U S A
; 102(48): 17366-71, 2005 Nov 29.
Article
em En
| MEDLINE
| ID: mdl-16301533
Vacuole biogenesis depends on specific targeting and retention of peripheral membrane proteins. At least three palmitoylated proteins are found exclusively on yeast vacuoles: the fusion factor Vac8, the kinase Yck3, and a novel adaptor protein implicated in microautophagy, Meh1. Here, we analyze the role that putative acyltransferases of the DHHC family play in their localization and function. We find that Pfa3/Ynl326c is required for efficient localization of Vac8 to vacuoles in vivo, while Yck3 or Meh1 localization is not impaired in any of the seven DHHC deletions. Vacuole-associated Vac8 appears to be palmitoylated in a pfa3 mutant, but this population is refractive to further palmitoylation on isolated vacuoles. Vacuole morphology and inheritance, which both depend on Vac8 palmitoylation, appear normal, although there is a reduction in vacuole fusion. Interestingly, Pfa3 is required for the vacuolar localization of not only an SH4 domain that is targeted by myristate/palmitate (as in Vac8) but also one that is targeted by a myristate/basic stretch (as in Src). Our data indicate that Pfa3 has an important but not exclusive function for Vac8 localization to the vacuole.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Palmitoil Coenzima A
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Saccharomyces cerevisiae
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Vacúolos
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Aciltransferases
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Proteínas de Saccharomyces cerevisiae
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Lipoproteínas
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Proteínas de Membrana
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Alemanha