A phosphatidylinositol/phosphatidylcholine transfer protein is required for differentiation of the dimorphic yeast Yarrowia lipolytica from the yeast to the mycelial form

doi:10.1083/jcb.125.1.113

This Article

	Full Text (PDF, 3871K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Lopez, M. C.
	Articles by Gaillardin, C.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Lopez, M. C.
	Articles by Gaillardin, C.


Social Bookmarking

	What's this?

ARTICLES

A phosphatidylinositol/phosphatidylcholine transfer protein is required for differentiation of the dimorphic yeast Yarrowia lipolytica from the yeast to the mycelial form

MC Lopez, JM Nicaud, HB Skinner, C Vergnolle, JC Kader, VA Bankaitis and C Gaillardin
Laboratoire de Genetique Moleculaire et Cellulaire, Institut National Agronomique Paris-Grignon, Thiverval-Grignon, France.

The SEC14SC gene encodes the phosphatidylinositol/phosphatidylcholine transfer protein (PI/PC-TP) of Saccharomyces cerevisiae. The SEC14SC gene product (SEC14pSC) is associated with the Golgi complex as a peripheral membrane protein and plays an essential role in stimulating Golgi secretory function. We report the characterization of SEC14YL, the structural gene for the PI/PC-TP of the dimorphic yeast Yarrowia lipolytica. SEC14YL encodes a primary translation product (SEC14YL) that is predicted to be a 497-residue polypeptide of which the amino- terminal 300 residues are highly homologous to the entire SEC14pSC, and the carboxyl-terminal 197 residues define a dispensible domain that is not homologous to any known protein. In a manner analogous to the case for SEC14pSC, SEC14pYL localizes to punctate cytoplasmic structures in Y. lipolytica that likely represent Golgi bodies. However, SEC14pYL is neither required for the viability of Y. lipolytica nor is it required for secretory pathway function in this organism. This nonessentiality of SEC14pYL for growth and secretion is probably not the consequence of a second PI/PC-TP activity in Y. lipolytica as cell-free lysates prepared from delta sec14YL strains are devoid of measurable PI/PC-TP activity in vitro. Phenotypic analyses demonstrate that SEC14pYL dysfunction results in the inability of Y. lipolytica to undergo the characteristic dimorphic transition from the yeast to the mycelial form that typifies this species. Rather, delta sec14YL mutants form aberrant pseudomycelial structures as cells enter stationary growth phase. The collective data indicate a role for SEC14pYL in promoting the differentiation of Y. lipolytica cells from yeast to mycelia, and demonstrate that PI/PC-TP function is utilized in diverse ways by different organisms.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Howe, A. G., Fairn, G. D., MacDonald, K., Bankaitis, V. A., McMaster, C. R. (2007). Regulation of Phosphoinositide Levels by the Phospholipid Transfer Protein Sec14p Controls Cdc42p/p21-Activated Kinase-Mediated Cell Cycle Progression at Cytokinesis. Eukaryot Cell 6: 1814-1823 [Abstract] [Full Text]
Dodds, P. N., Lawrence, G. J., Catanzariti, A.-M., Ayliffe, M. A., Ellis, J. G. (2004). The Melampsora lini AvrL567 Avirulence Genes Are Expressed in Haustoria and Their Products Are Recognized inside Plant Cells. Plant Cell 16: 755-768 [Abstract] [Full Text]
Alb, J. G. Jr., Phillips, S. E., Rostand, K., Cui, X., Pinxteren, J., Cotlin, L., Manning, T., Guo, S., York, J. D., Sontheimer, H., Collawn, J. F., Bankaitis, V. A. (2002). Genetic Ablation of Phosphatidylinositol Transfer Protein Function in Murine Embryonic Stem Cells. Mol. Biol. Cell 13: 739-754 [Abstract] [Full Text]
Kapranov, P., Routt, S. M., Bankaitis, V. A., de Bruijn, F. J., Szczyglowski, K. (2001). Nodule-Specific Regulation of Phosphatidylinositol Transfer Protein Expression in Lotus japonicus. Plant Cell 13: 1369-1382 [Abstract] [Full Text]
Hube, B., Hess, D., Baker, C. A., Schaller, M., Schäfer, W., Dolan, J. W. (2001). The role and relevance of phospholipase D1 during growth and dimorphism of Candida albicans. Microbiology 147: 879-889 [Abstract] [Full Text]
Weber, Y., Santore, U. J., Ernst, J. F., Swoboda, R. K. (2001). Divergence of Eukaryotic Secretory Components: the Candida albicans Homolog of the Saccharomyces cerevisiae Sec20 Protein Is N Terminally Truncated, and Its Levels Determine Antifungal Drug Resistance and Growth. J. Bacteriol. 183: 46-54 [Abstract] [Full Text]
Titorenko, V. I., Smith, J. J., Szilard, R. K., Rachubinski, R. A. (1998). Pex20p of the Yeast Yarrowia lipolytica Is Required for the Oligomerization of Thiolase in the Cytosol and for Its Targeting to the Peroxisome. JCB 142: 403-420 [Abstract] [Full Text]
Titorenko, V. I., Rachubinski, R. A. (1998). Mutants of the Yeast Yarrowia lipolytica Defective in Protein Exit from the Endoplasmic Reticulum Are Also Defective in Peroxisome Biogenesis. Mol. Cell. Biol. 18: 2789-2803 [Abstract] [Full Text]