Abstract
Cellular communication processes are highly dynamic and mediated, at least in part, by contacts between various membrane structures. The endoplasmic reticulum (ER), the major biosynthetic organelle of the cell, establishes an extensive network with other membrane structures to regulate the transport of intracellular molecules. Vacuole membrane protein 1 (VMP1), an ER-localized metazoan-specific protein, plays important roles in the formation of autophagosomes and communication between the ER and other organelles, including mitochondria, autophagosome precursor membranes, Golgi, lipid droplets, and endosomes. Increasing evidence has indicated that autophagy and ER–membrane communication at membrane contact sites are closely related to neurodegenerative disorders, such as Parkinson’s disease, Alzheimer’s disease, and amyotrophic lateral sclerosis. In this review, we summarize the roles of VMP1 in autophagy and ER–membrane contacts and discuss their potential implications in neurodegenerative disorders.
Highlights
Vacuole membrane protein 1 (VMP1), a pancreatitis-associated protein (Dusetti et al, 2002; Vaccaro et al, 2003), has attracted attention owing to its modulatory effects on membrane trafficking and autophagy
VMP1 has been shown to regulate endoplasmic reticulum (ER)–isolation membranes (IMs) contacts (Figure 2), and its depletion extends the duration of omegasomes, ER-associated autophagosome formation sites enriched in phosphatidylinositol 3-phosphate (PI3P) (Zhao et al, 2018)
Increasing evidences indicates that VMP1 plays important roles in autophagy by regulating the connections between the ER and IMs
Summary
Vacuole membrane protein 1 (VMP1), a pancreatitis-associated protein (Dusetti et al, 2002; Vaccaro et al, 2003), has attracted attention owing to its modulatory effects on membrane trafficking and autophagy. Roles of VMP1 in Autophagy and ER-Membrane Contact the highly dynamic nature of VMP1 puncta in concert with lipid droplets (LDs), mitochondria, and endosomes. VMP1 has been shown to regulate ER–IM contacts (Figure 2), and its depletion extends the duration of omegasomes, ER-associated autophagosome formation sites enriched in phosphatidylinositol 3-phosphate (PI3P) (Zhao et al, 2018).
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