Regulation of the transport and protein levels of the inositol phosphorylceramide mannosyltransferases Csg1 and Csh1 by the Ca2+-binding protein Csg2.

@article{Uemura2007RegulationOT,
  title={Regulation of the transport and protein levels of the inositol phosphorylceramide mannosyltransferases Csg1 and Csh1 by the Ca2+-binding protein Csg2.},
  author={Satoshi Uemura and Akio Kihara and Soichiro Iwaki and Jin-ichi Inokuchi and Yasuyuki Igarashi},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 12},
  pages={8613-21}
}
Complex sphingolipids in yeast are known to function in cellular adaptation to environmental changes. One of the yeast complex sphingolipids, mannosylinositol phosphorylceramide (MIPC), is produced by the redundant inositol phosphorylceramide (IPC) mannosyltransferases Csg1 and Csh1. The Ca2+-binding protein Csg2 can form a complex with either Csg1 or Csh1 and is considered to act as a regulatory subunit. However, the role of Csg2 in MIPC synthesis has remained unclear. In this study, we found… CONTINUE READING
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