Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Gene Ontology annotation based on curation of immunofluorescence data
Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells.
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Automatic assignment of GO terms using logical inference, based on inter-ontology links.
Combined Automated Annotation using Multiple IEA Methods.
Reduced expression of vacuole membrane protein 1 affects the invasion capacity of tumor cells.
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VMP1 was reported as a plasma membrane protein that participates in initial cell-cell contacts and tight junction formation, interacting with ZO-1/TJP1.
"We show for the first time that Vmp1 is a plasma membrane protein and an essential component of initial cell-cell contacts and tight junction formation. It interacts with the tight junction protein Zonula Occludens-1 and colocalizes in spots between neighboring HEK293 cells."
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Downregulation of VMP1 reduces cell adhesion and increases invasiveness.
"Downregulation of VMP1 by RNAi results in loss of cell adherence, and increases the invasion capacity of the non-invasive kidney cancer cell line Caki-2."
The TP53INP2 protein is required for autophagy in mammalian cells.
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TP53INP2 interacts with the autophagosome transmembrane protein VMP1, which is proposed to help recruit LC3/GABARAP proteins to the autophagosome membrane.
"TP53INP2 is a scaffold protein that recruits LC3 and/or LC3-related proteins to the autophagosome membrane by interacting with the transmembrane protein VMP1."
The VMP1-Beclin 1 interaction regulates autophagy induction.
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The VMP1 C-terminal hydrophilic domain binds the BH3 motif of Beclin 1, recruiting and activating the class III PI3K (hVps34) complex at the autophagosome formation site.
"This is achieved through its direct binding to the BH3 motif of Beclin 1 leading to the formation of a complex with the Class III phosphatidylinositol-3 kinase (PI3K) hVps34, a key positive regulator of autophagy, at the site where autophagosomes are generated."
The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity to Control ER-Isolation Membrane Contacts for Autophagosome Formation.
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VMP1 is an ER-localized autophagy protein that controls ER-isolation membrane contacts; its loss stably traps isolation membranes on the ER and blocks autophagosome formation.
"the ER-localized metazoan-specific autophagy protein EPG-3/VMP1 controls ER-IM contacts. Loss of VMP1 causes stable association of IMs with the ER, thus blocking autophagosome formation."
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VMP1 promotes SERCA activity by interacting with SERCA and preventing formation of the SERCA/PLN/SLN inhibitory complex, and modulates ER contacts with lipid droplets, mitochondria and endosomes.
"VMP1 interacts with SERCA and prevents formation of the SERCA/PLN/SLN inhibitory complex. VMP1 also modulates ER contacts with lipid droplets, mitochondria, and endosomes."
Genome-wide CRISPR screen identifies TMEM41B as a gene required for autophagosome formation.
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A genome-wide CRISPR screen identified TMEM41B, a VTT-domain protein related to VMP1, as required for autophagosome formation; VMP1 interacts with TMEM41B and shares the VTT domain.
"Genome-wide CRISPR screen identifies TMEM41B as a gene required for autophagosome formation."
CRISPR screening using an expanded toolkit of autophagy reporters identifies TMEM41B as a novel autophagy factor.
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A CRISPR screen using autophagy reporters identified TMEM41B (a VMP1 paralog) as required for phagophore maturation, supporting a shared role of VTT-domain ER proteins in autophagosome formation.
"TMEM41B, is required for phagophore maturation. TMEM41B is an integral endoplasmic reticulum"
A critical role of VMP1 in lipoprotein secretion.
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VMP1, but not other autophagy genes, is required for release of lipoproteins from the ER membrane into the ER lumen; its loss causes neutral lipid accumulation in the ER bilayer and impaired lipoprotein secretion.
"the release of lipoproteins from the ER membrane requires VMP1, an ER transmembrane protein essential for autophagy and certain types of secretion. Loss of vmp1, but not other autophagy-related genes, in zebrafish causes lipoprotein accumulation in the intestine and liver."
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In VMP1-depleted cells neutral lipids accumulate within the ER membrane bilayer, affecting lipoprotein secretion.
"In VMP1-depleted cells, neutral lipids accumulate within lipid bilayers of the ER membrane, thus affecting lipoprotein secretion."
A reference map of the human binary protein interactome.
A model for a partnership of lipid transfer proteins and scramblases in membrane expansion and organelle biogenesis.
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In vitro assays show VMP1 (with TMEM41B and ATG9) is a phospholipid scramblase that reequilibrates membrane leaflets; VMP1 and TMEM41B interact with the lipid transfer protein ATG2A.
"In vitro assays reveal TMEM41B, VMP1, and ATG9 as scramblases. We propose a model wherein membrane expansion results from the partnership of a lipid transfer protein, moving lipids between the cytosolic leaflets of apposed organelles, and scramblases that reequilibrate the leaflets of donor and acceptor organelle membranes as lipids are depleted or augmented."
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Purified VMP1 reconstituted into liposomes scrambles NBD-PE and NBD-PC, with no specificity to a particular glycerolipid; ATG2A is retained by both TMEM41B and VMP1.
"lipid scrambling by TMEM41B/VMP1, TMEM41B, and VMP1 are not specific to a particular glycerolipid (SI Appendix, Fig. 1D) as both NBD-PE and NBD-phosphatidylcholine (PC) are substrates."
TMEM41B and VMP1 are scramblases and regulate the distribution of cholesterol and phosphatidylserine.
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TMEM41B and VMP1 are phospholipid scramblases whose deficiency impairs the normal cellular distribution of cholesterol and phosphatidylserine.
"TMEM41B and VMP1 are phospholipid scramblases whose deficiency impairs the normal cellular distribution of cholesterol and phosphatidylserine."
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Purified VMP1 in liposomes scrambles NBD-PE, PC and PS; activity is ATP-independent and not affected by calcium and shows no headgroup specificity.
"The scramblase activity of TMEM41B/VMP1 did not depend on ATP and was not affected by calcium (Fig. S3, D and E). Of note, the scramblase activity of TMEM41B was not impacted by the presence of VMP1 (Fig. 4 B) and vice versa, indicating that TMEM41B's or VMP1's scramblase activity does not require the other in vitro. Moreover, no apparent specificity toward the head groups of phospholipids was detected"
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Deep research report on VMP1 (Q96GC9)
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VMP1 is an ER-resident DedA/VTT-domain phospholipid scramblase that cooperates with TMEM41B, ATG9 and ATG2 in autophagosome biogenesis and broader ER-derived membrane dynamics.
"VMP1 is a core ER scramblase that underpins autophagosome membrane biogenesis by cooperating with ATG2 and ATG9 and is broadly required for ER-derived membrane remodeling, including lipid droplets, lipoproteins, and viral DMVs"