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

Abstract

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.

• Authors: Robert H Michell, Stephen K Dove
• Journal: The EMBO journal (EMBO J) Vol. 28 Issue 2 Pg. 86-7 (Jan 21 2009) ISSN: 1460-2075 [Electronic] England
• PMID: 19158662 (Publication Type: Journal Article, Comment)

Chemical References

• 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

Topics

• Animals
• Autophagy-Related Proteins
• Flavoproteins (metabolism)
• Intracellular Signaling Peptides and Proteins (genetics, 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)