| Function |
Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (Probable). YPT7 is involved in regulation of vesicular protein transport in exo- and endocytosis (PubMed:8308065). Involved in homotypic vacuole fusion, the last step in the vacuole inheritance process, by interacting in its GTP-bound state on the donor membrane with the large multiprotein tethering complex termed HOPS on the acceptor membrane (PubMed:7489715, PubMed:11118206, PubMed:10725336, PubMed:10944212, PubMed:11210571, PubMed:19386605). Involved in the regulation of transport steps from late endosomes to the vacuole, mediated by interaction in its GTP-bound state on the donor membrane with the large multiprotein tethering complex termed class C-Vps complex on the acceptor membrane (PubMed:8308065, PubMed:11062257, PubMed:21062894). Involved in retromer assembly and cargo export, recognizing the cargo selection complex (CSC). GTP-bound YPT7 recruits CSC to vacuolar membranes via retromer subunit VPS35 (PubMed:22593205). Interacts with the HOPS complex subunit VPS39 independent of the HOPS complex at mitochondria-vacuole contact sites (vCLAMPs), providing a physical and metabolic interconnection between the endocytic pathway and mitochondria (PubMed:25026035).
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