ArticleThe EMBO journal2007
The ubiquitin-proteasome system regulates membrane fusion of yeast vacuoles.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Plant Cells under Attack: Unconventional Endomembrane Trafficking during Plant Defense.Plants (Basel, Switzerland) · 2020Review
- Cell Clearing Systems Bridging Neuro-Immunity and Synaptic Plasticity.International journal of molecular sciences · 2019Review
- Mutation-specific peripheral and ER quality control of hERG channel cell-surface expression.Scientific reports · 2019Article
- Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles.The Journal of biological chemistry · 2016Article
- The small GTPase EhRabB of Entamoeba histolytica is differentially expressed during phagocytosis.Parasitology research · 2013Article
- Saccharomyces cerevisiae Env7 is a novel serine/threonine kinase 16-related protein kinase and negatively regulates organelle fusion at the lysosomal vacuole.Molecular and cellular biology · 2013Article
- Molecular architecture and assembly of the eukaryotic proteasome.Annual review of biochemistry · 2013Review
- Article
- Characterizing ubiquitination sites by peptide-based immunoaffinity enrichment.Molecular & cellular proteomics : MCP · 2012Review
- Endosome maturation.The EMBO journal · 2011Review
- Sequential requirements for the GTPase domain of the mitofusin Fzo1 and the ubiquitin ligase SCFMdm30 in mitochondrial outer membrane fusion.Journal of cell science · 2011Article
- A novel membrane fusion-mediated plant immunity against bacterial pathogens.Genes & development · 2009Article
- Vps-C complexes: gatekeepers of endolysosomal traffic.Current opinion in cell biology · 2009Review
- Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase.The Journal of cell biology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Ubiquitination is known to regulate early stages of intracellular vesicular transport, without proteasomal involvement. We now show that, in yeast, ubiquitination regulates a late-stage, membrane fusion, with proteasomal involvement. A known proteasome mutant had a vacuolar fragmentation phenotype in vivo often associated with vacuolar membrane fusion defects, suggesting a proteasomal role in fusion. Inhibiting vacuolar proteasomes interfered with membrane fusion in vitro, showing that fusion cannot occur without proteasomal degradation. If so, one would expect to find ubiquitinated proteins on vacuolar membranes. We found a small number of these, identified the most prevalent one as Ypt7 and mapped its two major ubiquitination sites. Ubiquitinated Ypt7 was linked to the degradation event that is necessary for fusion: vacuolar Ypt7 and vacuolar proteasomes were interdependent, ubiquitinated Ypt7 became a proteasomal substrate during fusion, and proteasome inhibitors reduced fusion to greater degree when we decreased Ypt7 ubiquitination. The strongest model holds that fusion cannot proceed without proteasomal degradation of ubiquitinated Ypt7. As Ypt7 is one of many Rab GTPases, ubiquitin-proteasome regulation may be involved in membrane fusion elsewhere.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.