ArticlePloS one2011
VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 59 citations in OpenAlex.
- Molecular basis for the assembly of the Vps5-Vps17 SNX-BAR proteins with Retromer.Nature communications · 2025Article
- N-terminal signals in the SNX-BAR paralogs Vps5 and Vin1 guide endosomal coat complex formation.Molecular biology of the cell · 2024Article
- Diversity of retromer-mediated vesicular trafficking pathways in plants.Frontiers in plant science · 2023Review
- Receptor Recycling by Retromer.Molecular and cellular biology · 2023Review
- Article
- Mechanism of Gene-Environment Interactions Driving Glial Activation in Parkinson's Diseases.Current environmental health reports · 2021Review
- MPPED2 is downregulated in glioblastoma, and its restoration inhibits proliferation and increases the sensitivity to temozolomide of glioblastoma cells.Cell cycle (Georgetown, Tex.) · 2021Article
- Navigating the Controversies of Retromer-Mediated Endosomal Protein Sorting.Frontiers in cell and developmental biology · 2021Review
- Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29.Nature communications · 2020Article
- Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting.Journal of cell science · 2020Article
- Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism.Nature microbiology · 2020Article
- Manganese activates NLRP3 inflammasome signaling and propagates exosomal release of ASC in microglial cells.Science signaling · 2019Article
- Emerging Role of Retromer in Modulating Pathogen Growth.Trends in microbiology · 2018Review
- Inhibition of TBC1D5 activates Rab7a and can enhance the function of the retromer cargo-selective complex.Journal of cell science · 2018Article
- Retromer and the cation-independent mannose 6-phosphate receptor-Time for a trial separation?Traffic (Copenhagen, Denmark) · 2018Review
- Article
- SNX-1 and RME-8 oppose the assembly of HGRS-1/ESCRT-0 degradative microdomains on endosomes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Retromer Endosome Exit Domains Serve Multiple Trafficking Destinations and Regulate Local G Protein Activation by GPCRs.Current biology : CB · 2016Article
- The Role of Retromer in Alzheimer's Disease.Molecular neurobiology · 2016Review
- Unconventional endosome-like compartment and retromer complex in Toxoplasma gondii govern parasite integrity and host infection.Nature communications · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
VPS29 is a key component of the cargo-binding core complex of retromer, a protein assembly with diverse roles in transport of receptors within the endosomal system. VPS29 has a fold related to metal-binding phosphatases and mediates interactions between retromer and other regulatory proteins. In this study we examine the functional interactions of mammalian VPS29, using X-ray crystallography and NMR spectroscopy. We find that although VPS29 can coordinate metal ions Mn(2+) and Zn(2+) in both the putative active site and at other locations, the affinity for metals is low, and lack of activity in phosphatase assays using a putative peptide substrate support the conclusion that VPS29 is not a functional metalloenzyme. There is evidence that structural elements of VPS29 critical for binding the retromer subunit VPS35 may undergo both metal-dependent and independent conformational changes regulating complex formation, however studies using ITC and NMR residual dipolar coupling (RDC) measurements show that this is not the case. Finally, NMR chemical shift mapping indicates that VPS29 is able to associate with SNX1 via a conserved hydrophobic surface, but with a low affinity that suggests additional interactions will be required to stabilise the complex in vivo. Our conclusion is that VPS29 is a metal ion-independent, rigid scaffolding domain, which is essential but not sufficient for incorporation of retromer into functional endosomal transport assemblies.
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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.