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J. Biol. Chem., Vol. 283, Issue 8, 4730-4743, February 22, 2008

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Proteomic Analysis of a Nutritional Shift-up in Saccharomyces cerevisiae Identifies Gvp36 as a BAR-containing Protein Involved in Vesicular Traffic and Nutritional Adaptation^*

Lorenzo Querin¹², Rossella Sanvito¹³, Fulvio Magni, Stefano Busti, Alain Van Dorsselaer^¶, Lilia Alberghina, and Marco Vanoni¹⁴

From the Department of Biotechnology and Biosciences, University Milano-Bicocca, 20126 Milano, Italy, the University Milano-Bicocca, DIMESAB, 20052 Monza, Italy, and the ^¶CNRS, University Louis Pasteur, LSMBO, F-67070 Strasbourg, France

Yeast cells undergoing a nutritional shift-up from a poor to a rich carbon source take several hours to adapt to the novel, richer carbon source. The budding index is a physiologically relevant "global" parameter that reflects the complex links between cell growth and division that are both coordinately and deeply affected by nutritional conditions. We used changes in budding index as a guide to choose appropriate, relevant time points during an ethanol to glucose nutritional shift-up for preparation of samples for the analysis of proteome by two-dimensional electrophoresis/mass spectrometry. About 600 spots were detected. 90 spots, mostly comprising proteins involved in intermediary metabolism, protein synthesis, and response to stress, showed differential expression after glucose addition. Among modulated proteins we identified a protein of previously unknown function, Gvp36, showing a transitory increase corresponding to the drop of the fraction of budded cells. A gvp36 strain shares several phenotypes (including general growth defects, heat shock, and high salt sensitivity, defects in polarization of the actin cytoskeleton, in endocytosis and in vacuolar biogenesis, defects in entering stationary phase upon nutrient starvation) with secretory pathway mutants and with mutants in genes encoding the two previously known yeast BAR proteins (RSV161 and RSV167). We thus propose that Gvp36 represents a novel yeast BAR protein involved in vesicular traffic and in nutritional adaptation.

Received for publication, September 17, 2007 , and in revised form, December 21, 2007.

^* This work was supported by grants from Ministero dell'Universitá e della Ricerca (MIUR) (Fondo per le Agevolazioni alla Ricerca and COFIN2006) (to M. V.) and MIUR (Fondo per gli Investimenti della Ricerca di Base-ITALBionet) (to L. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1-S8 and Tables S1-S4.

¹ Contributed equally to this work.

² Present address: DiaSorin S.p.A., c/o Nerviano Medical Science, Viale Pasteur 10, 20014 Nerviano, Italy.

³ Present address: Merck Serono S.p.A., Structural Characterization Lab., Via Valle Caia 22, 00040 Ardea, Italy.

⁴ To whom correspondence should be addressed: Piazza della Scienza 2, 20126 Milano, Tel.: 39-02-64483525; Fax: 39-02-64483519; E-mail: marco.vanoni{at}unimib.it.

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