ArticleMolecular biology of the cell2017
How and why intralumenal membrane fragments form during vacuolar lysosome fusion.
Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- From "lysosomal addiction" to targeted therapies: exploiting novel windows in colorectal cancer.European journal of medical research · 2025Review
- Mfn2-dependent fusion pathway of PE-enriched micron-sized vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A hemifused complex is the hub in a network of pathways to membrane fusion.Biophysical journal · 2023Article
- Membrane Fusion Mediated by Non-covalent Binding of Re-engineered Cholera Toxin Assemblies to Glycolipids.ACS synthetic biology · 2022Article
- A two-tiered system for selective receptor and transporter protein degradation.PLoS genetics · 2022Article
- Organelle tethering, pore formation and SNARE compensation in the late endocytic pathway.Journal of cell science · 2021Article
- Through the back door: Unconventional protein secretion.Cell surface (Amsterdam, Netherlands) · 2020Review
- The Participation of Regulatory Lipids in Vacuole Homotypic Fusion.Trends in biochemical sciences · 2019Review
- HOPS-dependent endosomal fusion required for efficient cytosolic delivery of therapeutic peptides and small proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The intralumenal fragment pathway mediates ESCRT-independent surface transporter down-regulation.Nature communications · 2018Article
- SNARE-mediated membrane fusion arrests at pore expansion to regulate the volume of an organelle.The EMBO journal · 2018Article
- Evidence for ESCRT- and clathrin-dependent microautophagy.The Journal of cell biology · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysosomal membrane fusion mediates the last step of the autophagy and endocytosis pathways and supports organelle remodeling and biogenesis. Because fusogenic proteins and lipids concentrate in a ring at the vertex between apposing organelle membranes, the encircled area of membrane can be severed and internalized within the lumen as a fragment upon lipid bilayer fusion. How or why this intralumenal fragment forms during fusion, however, is not entirely clear. To better understand this process, we studied fragment formation during homotypic vacuolar lysosome membrane fusion in Saccharomyces cerevisiae Using cell-free fusion assays and light microscopy, we find that GTPase activation and trans-SNARE complex zippering have opposing effects on fragment formation and verify that this affects the morphology of the fusion product and regulates transporter protein degradation. We show that fragment formwation is limited by stalk expansion, a key intermediate of the lipid bilayer fusion reaction. Using electron microscopy, we present images of hemifusion diaphragms that form as stalks expand and propose a model describing how the fusion machinery regulates fragment formation during lysosome fusion to control morphology and protein lifetimes.
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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.