ArticleMolecular biology of the cell2016
Yeast Vps13 promotes mitochondrial function and is localized at membrane contact sites.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers, 1 of them a synthesis that pooled it.
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Who cites it
107 citing papers in PubMed, 1 synthesis or guideline pooled it, 173 citations in OpenAlex.
- Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024Pooled it
- Mitochondria-endoplasmic reticulum-lipid droplet crosstalk in lipid metabolic reprogramming in type 2 diabetes mellitus.Journal of lipid research · 2026Review
- Functional diversification across yeast lineages of the nucleus-vacuole junction forming protein Nvj1.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms and Therapeutic Potential of Targeting Mitophagy in Neurodegenerative Diseases.Molecular neurobiology · 2026Review
- Mitochondrially tethered Mmm1 can function as a sole lipid transporter at ER-mitochondria contacts.The Journal of cell biology · 2026Article
- Four subtypes of disease-causing missense mutations underlie pathogenic protein interactions in neurodegenerative VPS13A disease.The Journal of clinical investigation · 2026Article
- Hoi1 targets BLTP2 to ER-PM contact sites to regulate lipid homeostasis.The Journal of cell biology · 2026Article
- Transport of sphingolipids by yeast Npc2 supports phase separation of the vacuole membrane.The Journal of biological chemistry · 2026Article
- VPS13B recruits lipid vesicles to promote mitochondrial fission and quality control.Nature communications · 2025Article
- BLTP3A is associated with membranes of the late endocytic pathway and is an effector of CASM.The EMBO journal · 2025Article
- Transport of sphingolipids by yeast Npc2 supports phase separation of the vacuole membrane.bioRxiv : the preprint server for biology · 2025Article
- Neurodegenerative and Neurodevelopmental Roles for Bulk Lipid Transporters VPS13A and BLTP2.Movement disorders : official journal of the Movement Disorder Society · 2025Article
- An origin for a eukaryotic lipid transfer protein fold in Asgard archaea.bioRxiv : the preprint server for biology · 2025Article
- Suppression of plastid-to-nucleus gene transfer by DNA double-strand break repair.Nature plants · 2025Article
- A brief history of phosphatidylinositol transfer proteins: from the backwaters of cell biology to prime time in lipid signaling.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025Review
- Roles of non-specific lipid transfer proteins in plant defense: structural and functional perspectives.Frontiers in fungal biology · 2025Review
- Red blood cell lipid distribution in the pathophysiology and laboratory evaluation of chorea-acanthocytosis and McLeod syndrome patients.Frontiers in physiology · 2025Article
- Remodeling of the secretory pathway is coordinated withiScience · 2024Article
- Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024Review
- Mitofusin-mediated contacts between mitochondria and peroxisomes regulate mitochondrial fusion.PLoS biology · 2024Article
47 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The Vps13 protein family is highly conserved in eukaryotic cells. Mutations in human VPS13 genes result in a variety of diseases, such as chorea acanthocytosis (ChAc), but the cellular functions of Vps13 proteins are not well defined. In yeast, there is a single VPS13 orthologue, which is required for at least two different processes: protein sorting to the vacuole and sporulation. This study demonstrates that VPS13 is also important for mitochondrial integrity. In addition to preventing transfer of DNA from the mitochondrion to the nucleus, VPS13 suppresses mitophagy and functions in parallel with the endoplasmic reticulum-mitochondrion encounter structure (ERMES). In different growth conditions, Vps13 localizes to endosome-mitochondrion contacts and to the nuclear-vacuole junctions, indicating that Vps13 may function at membrane contact sites. The ability of VPS13 to compensate for the absence of ERMES correlates with its intracellular distribution. We propose that Vps13 is present at multiple membrane contact sites and that separation-of-function mutants are due to loss of Vps13 at specific junctions. Introduction of VPS13A mutations identified in ChAc patients at cognate sites in yeast VPS13 are specifically defective in compensating for the lack of ERMES, suggesting that mitochondrial dysfunction might be the basis for ChAc.
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