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The Vps13 protein family is highly conserved in eukaryotic cells. In humans, mutations in the gene encoding the family member  VPS13A  lead to the neurodegenerative disorder chorea-acanthocytosis. In the yeast  Saccharomyces cerevisiae , there is just a single version of  VPS13 , thereby simplifying the task of unraveling its molecular function(s). While  VPS13  was originally identified in yeast by its role in vacuolar sorting, recent studies have revealed a completely different function for  VPS13  in sporulation, where  VPS13  regulates phosphatidylinositol-4-phosphate (PtdIns(4)P) levels in the prospore membrane. This discovery raises the possibility that the disease phenotype associated with  vps13A  mutants in humans is due to misregulation of PtdIns(4)P in membranes. To determine whether  VPS13A  affects PtdIns(4)P in membranes from mammalian neuronal cells, phosphatidylinositol phosphate pools were compared in PC12 tissue culture cells in the absence or presence of  VPS13A . Consistent with the yeast results, the localization of PtdIns(4)P is specifically altered in  VPS13A  knockdown cells while other phosphatidylinositol phosphates appear unaffected. In addition,  VPS13A  is necessary to prevent the premature degeneration of neurites that develop in response to Nerve Growth Factor. The regulation of PtdIns(4)P is therefore a conserved function of the Vps13 family and may play a role in the maintenance of neuronal processes in mammals.

A Conserved Function in Phosphatidylinositol Metabolism for Mammalian Vps13 Family Proteins