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Eukaryotic Cell, February 2005, p. 281-288, Vol. 4, No. 2
1535-9778/05/$08.00+0     doi:10.1128/EC.4.2.281-288.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Interaction among Btn1p, Btn2p, and Ist2p Reveals Potential Interplay among the Vacuole, Amino Acid Levels, and Ion Homeostasis in the Yeast Saccharomyces cerevisiae

Yoojin Kim,1,{dagger} Subrata Chattopadhyay,1 Sarahjane Locke,1 and David A. Pearce1,2,3*

Center for Aging and Developmental Biology, Aab Institute of Biomedical Sciences,1 Department of Biochemistry and Biophysics,2 Department of Neurology, School of Medicine and Dentistry, University of Rochester, Rochester, New York3

Received 12 August 2004/ Accepted 11 November 2004

Btn2p, a novel cytosolic coiled-coil protein in Saccharomyces cerevisiae, was previously shown to interact with and to be necessary for the correct localization of Rhb1p, a regulator of arginine uptake, and Yif1p, a Golgi protein. We now report the biochemical and physical interactions of Btn2p with Ist2p, a plasma membrane protein that is thought to have a function in salt tolerance. A deletion in Btn2p (btn2{Delta} strains) results in a failure to correctly localize Ist2p, and strains lacking Btn2p and Ist2p (btn2{Delta} ist2{Delta} strains) are unable to grow in the presence of 0.5 or 1.0 M NaCl. Btn2p was originally identified as being up-regulated in a btn1{Delta} strain, which lacks the vacuolar-lysosomal membrane protein, Btn1p, and serves as a model for Batten disease. This up-regulation of Btn2p was shown to contribute to the maintenance of a stable vacuolar pH in the btn1{Delta} strain. Btn1p was subsequently shown to be required for the optimal transport of arginine into the vacuole. Interestingly, btn1{Delta} ist2{Delta} strains are also unable to grow in the presence of 0.5 or 1.0 M NaCl, and ist2{Delta} suppresses the vacuolar arginine transport defect in btn1{Delta} strains. Although further investigation is required, we speculate that altered vacuolar arginine transport in btn1{Delta} strains represents a mechanism for maintaining or balancing cellular ion homeostasis. Btn2p interacts with at least three proteins that are seemingly involved in different biological functions in different subcellular locations. Due to these multiple interactions, we conclude that Btn2p may play a regulatory role across the cell in response to alterations in the intracellular environment that may be caused by changes in amino acid levels or pH, a disruption in protein trafficking, or imbalances in ion homeostasis resulting from either genetic or environmental manipulation.

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

{dagger} Present address: Vollum Institute, Oregon Health Sciences University, Portland, OR 97239.

Eukaryotic Cell, February 2005, p. 281-288, Vol. 4, No. 2
1535-9778/05/$08.00+0     doi:10.1128/EC.4.2.281-288.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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