Hou, Haitong and Subramanian, Kanagaraj and LaGrassa, Tracy J. and Markgraf, Daniel and Dietrich, Lars E. P. and Urban, Jörg and Decker, Nadine and Ungermann, Christian (2005) The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8. Proceedings of the National Academy of Sciences of the United States of America, 102 (48). pp. 17366-17371. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:HOUpnas05
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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.
|Additional Information:||Copyright © 2005 by the National Academy of Sciences Communicated by William T. Wickner, Dartmouth Medical School, Hanover, NH, October 11, 2005 (received for review September 26, 2005) Published online before print November 21, 2005, 10.1073/pnas.0508885102 We thank Christoph Meiringer, Clemens Ostrowicz, and Karolina Peplowska for comments; Gabriela Müller for expert technical assistance; and Sean Munro and Michael Knop for plasmids. This work was supported by Deutsche Forschungsgemeinschaft Grant UN111/3-1 (Heisenberg Program), Sonderforschungsbereich 638, the EMBO Young Investigator Program, and Fonds der Chemischen Industrie. T.J.L. was the recipient of a predoctoral fellowship from the National Science Foundation. L.E.P.D. was a recipient of a predoctoral fellowship from the Boehringer Ingelheim Fonds. Conflict of interest statement: No conflicts declared. H.H., K.S., and T.J.L. contributed equally to this work.|
|Subject Keywords:||Yck3; SH4 domain; acylation; membrane targeting|
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|Deposited By:||Archive Administrator|
|Deposited On:||01 Jan 2007|
|Last Modified:||26 Dec 2012 09:26|
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