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.
MeSH terms
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Animals
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Autophagy-Related Proteins
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Flavoproteins / metabolism
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Intracellular Signaling Peptides and Proteins / genetics
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Intracellular Signaling Peptides and Proteins / metabolism
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Membrane Proteins / metabolism
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Mice
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Mutation
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Osmotic Pressure
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Phosphatidylinositol Phosphates / biosynthesis*
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Phosphoric Monoester Hydrolases
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Phosphotransferases (Alcohol Group Acceptor) / metabolism
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Protein Transport
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Saccharomyces cerevisiae Proteins / metabolism
Substances
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ATG18 protein, S cerevisiae
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Autophagy-Related Proteins
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Flavoproteins
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Phosphatidylinositol Phosphates
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Saccharomyces cerevisiae Proteins
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VAC7 protein, S cerevisiae
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Vac14 protein, mouse
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phosphatidylinositol 3,5-diphosphate
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FAB1 protein, S cerevisiae
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Phosphotransferases (Alcohol Group Acceptor)
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FIG4 protein, S cerevisiae
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Phosphoric Monoester Hydrolases