Mammalian inositol polyphosphate 5-phosphatase II can compensate for the absence of all three yeast Sac1-like-domain-containing 5-phosphatases.

@article{OMalley2001MammalianIP,
  title={Mammalian inositol polyphosphate 5-phosphatase II can compensate for the absence of all three yeast Sac1-like-domain-containing 5-phosphatases.},
  author={Cindy J. O’Malley and Bradley K McColl and Anne M Kong and S L Ellis and A P Wijayaratnam and Joseph Sambrook and Christina A Mitchell},
  journal={The Biochemical journal},
  year={2001},
  volume={355 Pt 3},
  pages={
          805-17
        }
}
  • Cindy J. O’Malley, Bradley K McColl, +4 authors Christina A Mitchell
  • Published in The Biochemical journal 2001
  • Biology, Medicine
  • Phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P(2)] plays a complex role in generating intracellular signalling molecules, and also in regulating actin-binding proteins, vesicular trafficking and vacuolar fusion. Four inositol polyphosphate 5-phosphatases (hereafter called 5-phosphatases) have been identified in Saccharomyces cerevisiae: Inp51p, Inp52p, Inp53p and Inp54p. Each enzyme contains a 5-phosphatase domain which hydrolyses PtdIns(4,5)P(2), forming PtdIns4P, while Inp52p and Inp53p… CONTINUE READING

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    Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast.