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Eukaryotic Cell, August 2002, p. 606-612, Vol. 1, No. 4
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.4.606-612.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Interaction with Btn2p Is Required for Localization of Rsg1p: Btn2p-Mediated Changes in Arginine Uptake in Saccharomyces cerevisiae

Subrata Chattopadhyay1 and David A. Pearce1,2*

Center for Aging and Developmental Biology,1 Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 146422

Received 13 February 2002/ Accepted 19 April 2002

Btn2p, a novel coiled-coil protein, is up-regulated in btn1{Delta} yeast strains, and this up-regulation is thought to contribute to maintaining a stable vacuolar pH in btn1{Delta} strains (D. A. Pearce, T. Ferea, S. A. Nosel, B. Das, and F. Sherman, Nat. Genet. 22:55-58, 1999). We now report that Btn2p interacts biochemically and functionally with Rsg1p, a down-regulator of the Can1p arginine and lysine permease. Rsg1p localizes to a distinct structure toward the cell periphery, and strains lacking Btn2p (btn2{Delta} strains) fail to correctly localize Rsg1p. btn2{Delta} strains, like rsg1{Delta} strains, are sensitive for growth in the presence of the arginine analog canavanine. Furthermore, btn2{Delta} strains, like rsg1{Delta} strains, demonstrate an elevated rate of uptake of [14C]arginine, which leads to increased intracellular levels of arginine. Overexpression of BTN2 results in a decreased rate of arginine uptake. Collectively, these results indicate that altered levels of Btn2p can modulate arginine uptake through localization of the Can1p-arginine permease regulatory protein, Rsg1p. Our original identification of Btn2p was that it is up-regulated in the btn1{Delta} strain which serves as a model for the lysosomal storage disorder Batten disease. Btn1p is a vacuolar/lysosomal membrane protein, and btn1{Delta} suppresses both the canavanine sensitivity and the elevated rate of uptake of arginine displayed by btn2{Delta} rsg1{Delta} strains. We conclude that Btn2p interacts with Rsg1p and modulates arginine uptake. Up-regulation of BTN2 expression in btn1{Delta} strains may facilitate either a direct or indirect effect on intracellular arginine levels.

* Corresponding author. Mailing address: Center for Aging and Developmental Biology, Department of Biochemistry and Biophysics, Box 645, University of Rochester, School of Medicine and Dentistry, Rochester, NY 14642. Phone: (585) 273-1514. Fax: (585) 506-1972. E-mail: david_pearce{at}urmc.rochester.edu.

Eukaryotic Cell, August 2002, p. 606-612, Vol. 1, No. 4
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.4.606-612.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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