ArticleJournal of cell science2014
RME-8 coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation.
Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 111 citations in OpenAlex.
- Retromer-targeted therapy for neurodegenerative diseases.Molecular neurodegeneration · 2026Review
- Structural Mechanisms of DNAJC13 Dimeric Assembly and InsPbioRxiv : the preprint server for biology · 2026Article
- Distinct Rab11-associated membrane trafficking pathways bidirectionally control neuronal extracellular vesicle cargo traffic.bioRxiv : the preprint server for biology · 2026Article
- Association of the endosomal sorting processes cargo selection and membrane tubulation with human reward system reactivity.European archives of psychiatry and clinical neuroscience · 2026Article
- Neddylation-dependent RAB40-Cullin5 E3 ligase complex controls ubiquitin-mediated proteasomal degradation of DNAJC13.BBA advances · 2026Article
- The actin nucleation promoting factor WASH facilitates clathrin-independent endocytosis of human papillomaviruses.EMBO reports · 2025Article
- DNAJC13 localization to endosomes is opposed by its J domain and its disordered C-terminus.Molecular biology of the cell · 2025Article
- Ubiquitination Regulates Reorganization of the Membrane System During Cytomegalovirus Infection.Life (Basel, Switzerland) · 2025Article
- Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation.Nature communications · 2025Article
- The Parkinson Disease-Associated Mutant DNAJC13(N855S) Leads to Its Accelerated Degradation and Negatively Affects Macroautophagy and Retromer Complex-Mediated Dynamics.Journal of cellular physiology · 2025Article
- An engineered trafficking biosensor reveals a role for DNAJC13 in DOR downregulation.Nature chemical biology · 2025Article
- DNAJC13 localization to endosomes is opposed by its J domain and its disordered C-terminal tail.bioRxiv : the preprint server for biology · 2024Article
- Assembly and fission of tubular carriers mediating protein sorting in endosomes.Nature reviews. Molecular cell biology · 2024Review
- Structural basis for coupling of the WASH subunit FAM21 with the endosomal SNX27-Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- VPS35 and retromer dysfunction in Parkinson's disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Architecture of the ESCPE-1 membrane coat.Nature structural & molecular biology · 2023Article
- Out of the ESCPE room: Emerging roles of endosomal SNX-BARs in receptor transport and host-pathogen interaction.Traffic (Copenhagen, Denmark) · 2023Review
- Parkinson's disease: From genetics to molecular dysfunction and targeted therapeutic approaches.Genes & diseases · 2023Review
- FAM21 is critical for TLR2/CLEC4E-mediated dendritic cell function againstLife science alliance · 2023Article
- Cell-specific secretory granule sorting mechanisms: the role of MAGEL2 and retromer in hypothalamic regulated secretion.Frontiers in cell and developmental biology · 2023Review
10 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Retromer is a vital element of the endosomal protein sorting machinery and comprises two subcomplexes that operate together to sort membrane proteins (cargo) and tubulate membranes. Tubules are formed by a dimer of sorting nexins, a key component of which is SNX1. Cargo selection is mediated by the VPS35-VPS29-VPS26 trimer, which additionally recruits the WASH complex through VPS35 binding to the WASH complex subunit FAM21. Loss of function of the WASH complex leads to dysregulation of endosome tubulation, although it is unclear how this occurs. Here, we show that FAM21 also binds to the SNX1-interacting DNAJ protein RME-8. Loss of RME-8 causes altered kinetics of SNX1 membrane association and a pronounced increase in highly branched endosomal tubules. Building on previous observations from other laboratories, we show that these tubules contain membrane proteins that are dependent upon WASH complex activity for their localization to the plasma membrane. Therefore, we propose that the interaction between RME-8 and the WASH complex provides a means to coordinate the activity of the WASH complex with the membrane-tubulating function of the sorting nexins at sites where retromer-mediated endosomal protein sorting occurs.
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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.