| Primary Identifier | IPR056748 | Type | Domain |
| Short Name | VPS13-like_C |
| description | This entry represents the C-terminal PH-like domain from VPS13 which weakly binds to phosphatidylinositol 4,5-bisphosphate and contributes to membrane recruitment [, , ]. Truncation of this domain in VPS13A are causative for chorea-acanthocytosis, which suggests that it plays an important function [].VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. VPS13A, VPS13C and VPS13D from mammals localise at contacts at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localise to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia []. |
