Interaction with Btn2p is required for localization of Rsglp: Btn2p-mediated changes in arginine uptake in Saccharomyces cerevisiae.

@article{Chattopadhyay2002InteractionWB,
  title={Interaction with Btn2p is required for localization of Rsglp: Btn2p-mediated changes in arginine uptake in Saccharomyces cerevisiae.},
  author={Subrata Chattopadhyay and David A. Pearce},
  journal={Eukaryotic cell},
  year={2002},
  volume={1 4},
  pages={606-12}
}
Btn2p, a novel coiled-coil protein, is up-regulated in btn1delta yeast strains, and this up-regulation is thought to contribute to maintaining a stable vacuolar pH in btn1delta 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 Rsglp, a down-regulator of the Can1p arginine and lysine permease. Rsglp localizes to a distinct structure toward the cell periphery, and strains… CONTINUE READING

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