The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8

Autor(en): Hou, HT
Subramanian, K
LaGrassa, TJ
Markgraf, D
Dietrich, LEP
Urban, J
Decker, N
Ungermann, C 
Stichwörter: acylation; ACYLTRANSFERASE; HOMOLOG; IDENTIFICATION; INHERITANCE; LOCALIZATION; membrane targeting; Multidisciplinary Sciences; SACCHAROMYCES-CEREVISIAE; Science & Technology - Other Topics; SH4 domain; SNARE COMPLEX; TRAFFICKING; TRANSFERASE; Yck3; YEAST
Erscheinungsdatum: 2005
Herausgeber: NATL ACAD SCIENCES
Journal: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volumen: 102
Ausgabe: 48
Startseite: 17366
Seitenende: 17371
Zusammenfassung: 
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.
ISSN: 00278424
DOI: 10.1073/pnas.0508885102

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