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| Proc. Natl. Acad. Sci. U.S.A. Nov (2005); 102(48):17366-71 | |
| The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8- | |
| Hou H, Subramanian K, LaGrassa TJ, Markgraf D, Dietrich LE, Urban J, Decker N, Ungermann C | |
| Biochemie-Zentrum der Universitat Heidelberg, Germany- | |
| Abstract: 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- | |
| [PUBMED: 16301533] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |