Phosphatidylinositol/phosphatidylcholine transfer proteins in yeast

Biochim Biophys Acta. 2000 Jun 26;1486(1):55-71. doi: 10.1016/s1388-1981(00)00048-2.

Abstract

Phosphatidylinositol transfer proteins (PITPs) are now becoming widely recognized as intriguing proteins that participate in the coordination and coupling of phospholipid metabolism with vesicle trafficking, and in the regulation of important signaling cascades. Yet, only in one case is there a large body of evidence that speaks to the precise identities of PITP-dependent cellular reactions, and to the mechanisms by which PITPs execute function in eukaryotic cells. At present, yeast provide the most powerful system for analysis of the physiology of PITP function in vivo, and the mechanism by which this function is carried out. Here, we review the recent progress and remaining questions in the area of PITP function in yeast.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Biological Transport
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Fungal Proteins / metabolism
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Molecular Structure
  • Mutation
  • Nitrogenous Group Transferases / genetics
  • Phosphatidylcholines / metabolism*
  • Phosphatidylinositols / metabolism*
  • Phospholipid Transfer Proteins
  • Phosphoric Monoester Hydrolases
  • Receptors, Steroid
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid

Substances

  • Carrier Proteins
  • Fungal Proteins
  • KES1 protein, S cerevisiae
  • Membrane Proteins
  • Phosphatidylcholines
  • Phosphatidylinositols
  • Phospholipid Transfer Proteins
  • Receptors, Steroid
  • SEC14L1 protein, human
  • SEC24 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Nitrogenous Group Transferases
  • glycerophosphorylcholine synthetase
  • SAC1 protein, S cerevisiae
  • Phosphoric Monoester Hydrolases