A protein complex that regulates PtdIns(3,5)P2 levels

EMBO J. 2009 Jan 21;28(2):86-7. doi: 10.1038/emboj.2008.270.


Phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) is needed for retrograde membrane trafficking from lysosomal and late endosomal compartments and its synthesis is tightly regulated. But how cells regulate PtdIns(3,5)P2 synthesis--for example, in response to hyperosmotic shock--remains unexplained. A paper from the Weisman group gives the most complete picture so far of a multiprotein complex that controls PtdIns(3,5)P2 synthesis and explains how a VAC14 mutation functionally impairs the scaffold protein at the heart of the complex and causes a neurodegenerative condition in mice.

Publication types

  • Comment

MeSH terms

  • Animals
  • Autophagy-Related Proteins
  • Flavoproteins / metabolism
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Membrane Proteins / metabolism
  • Mice
  • Mutation
  • Osmotic Pressure
  • Phosphatidylinositol Phosphates / biosynthesis*
  • Phosphoric Monoester Hydrolases
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Protein Transport
  • Saccharomyces cerevisiae Proteins / metabolism


  • ATG18 protein, S cerevisiae
  • Autophagy-Related Proteins
  • Flavoproteins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Phosphatidylinositol Phosphates
  • Saccharomyces cerevisiae Proteins
  • VAC7 protein, S cerevisiae
  • Vac14 protein, mouse
  • phosphatidylinositol 3,5-diphosphate
  • FAB1 protein, S cerevisiae
  • Phosphotransferases (Alcohol Group Acceptor)
  • FIG4 protein, S cerevisiae
  • Phosphoric Monoester Hydrolases