ArticleThe Biochemical journal2007
Identification of a conserved motif required for Vps35p/Vps26p interaction and assembly of the retromer complex.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
- VPS35-Retromer: Multifunctional Roles in Various Biological Processes - A Focus on Neurodegenerative Diseases and Cancer.Journal of inflammation research · 2025Review
- VPS35 or retromer as a potential target for neurodegenerative disorders: barriers to progress.Expert opinion on therapeutic targets · 2024Review
- VPS35 and retromer dysfunction in Parkinson's disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Receptor Recycling by Retromer.Molecular and cellular biology · 2023Review
- WDR91 specifies the endosomal retrieval subdomain for retromer-dependent recycling.The Journal of cell biology · 2022Article
- Understanding the contributions of VPS35 and the retromer in neurodegenerative disease.Neurobiology of disease · 2022Review
- The retromer is co-opted to deliver lipid enzymes for the biogenesis of lipid-enriched tombusviral replication organelles.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Retromer retrieves the Wilson disease protein ATP7B from endolysosomes in a copper-dependent manner.Journal of cell science · 2020Article
- Retromer has a selective function in cargo sorting via endosome transport carriers.The Journal of cell biology · 2019Article
- Where no Ras has gone before: VPS35 steers N-Ras through the cytosol.Small GTPases · 2019Article
- Updated Insight into the Physiological and Pathological Roles of the Retromer Complex.International journal of molecular sciences · 2017Review
- VPS35, the Retromer Complex and Parkinson's Disease.Journal of Parkinson's disease · 2017Review
- Article
- Structural and mechanistic insights into regulation of the retromer coat by TBC1d5.Nature communications · 2016Article
- VPS35 binds farnesylated N-Ras in the cytosol to regulate N-Ras trafficking.The Journal of cell biology · 2016Article
- Role of the Retromer Complex in Neurodegenerative Diseases.Frontiers in aging neuroscience · 2016Review
- Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy.Nature communications · 2014Article
- RME-8 coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation.Journal of cell science · 2014Article
- Retromer association with membranes: plants have their own rules!Plant signaling & behavior · 2013Article
- Mechanisms governing the endosomal membrane recruitment of the core retromer in Arabidopsis.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The retromer complex is a conserved cytoplasmic coat complex that mediates the endosome-to-Golgi retrieval of vacuole/lysosome hydrolase receptors in yeast and mammals. The recognition of cargo proteins by the retromer is performed by the Vps35p/VPS35 (where Vps is vacuolar protein sorting) component, which together with Vps26p/VPS26 and Vps29p/VPS29, forms the cargo-selective subcomplex. In this report, we have identified a highly-conserved region of Vps35p/VPS35 that is essential for the interaction with Vps26p/VPS26 and for assembly of the retromer complex. Mutation of residues within the conserved region results in Vps35p/VPS35 mutants, which cannot bind to Vps26p/VPS26 and are not efficiently targeted to the endosomal membrane. These data implicate Vps26p/VPS26 in regulating Vps35p/VPS35 membrane association and therefore suggest a role for Vps26p/VPS26 in cargo recognition.
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What OpenQuestion holds
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.