Efficient ER exit and vacuole targeting of yeast Sna2p require two tyrosine-based sorting motifs.

@article{Renard2010EfficientEE,
  title={Efficient ER exit and vacuole targeting of yeast Sna2p require two tyrosine-based sorting motifs.},
  author={H. Renard and Didier Demaegd and B{\'e}reng{\`e}re Guerriat and Pierre Morsomme},
  journal={Traffic},
  year={2010},
  volume={11 7},
  pages={931-46}
}
SNA (Sensitive to Na(+)) proteins form a membrane protein family, which, in the yeast Saccharomyces cerevisiae, is composed of four members: Sna1p/Pmp3p, Sna2p, Sna3p and Sna4p. In this study, we focused on the 79 residue Sna2p protein. We found that Sna2p is localized in the vacuolar membrane. Directed mutagenesis showed that two functional tyrosine motifs YXXØ are present in the C-terminal region. Each of these is involved in a different Golgi-to-vacuole targeting pathway: the tyrosine 65… CONTINUE READING
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Binding to Rsp5p targets to the endosomal pathway the yeast Sna3p, a protein ubiquitylated with Lysine-63-linked chains. Traffic 2007;8:1280–1296

  • M Stawiecka-Mirota, W Pokrzywa, +4 authors P. Morsomme
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Binding to Rsp 5 p targets to the endosomal pathway the yeast Sna 3 p , a protein ubiquitylated with Lysine - 63 - linked chains

  • M Stawiecka-Mirota, W Pokrzywa, +4 authors P Morsomme
  • Traffic
  • 2007

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