ArticleThe Biochemical journal2006
The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 52 citations in OpenAlex.
- Identification of a VPS29 isoform with restricted association to Retriever and Retromer accessory proteins through autoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Chemical genomic analysis reveals the interplay between iron chelation, zinc homeostasis, and retromer function in the bioactivity of an ethanol adduct of the feijoa fruit-derived ellagitannin vescalagin.G3 (Bethesda, Md.) · 2024Article
- The retromer and retriever systems are conserved and differentially expanded in parabasalids.Journal of cell science · 2024Article
- EhVps35, a retromer component, is involved in the recycling of the EhADH and Gal/GalNac virulent proteins ofFrontiers in parasitology · 2024Article
- Article
- Molecular characterization and protective efficacy of vacuolar protein sorting 29 fromFrontiers in cellular and infection microbiology · 2023Article
- Receptor Recycling by Retromer.Molecular and cellular biology · 2023Review
- Navigating the Controversies of Retromer-Mediated Endosomal Protein Sorting.Frontiers in cell and developmental biology · 2021Review
- How Reversible Are the Effects of Fumed Silica on Macrophages? A Proteomics-Informed View.Nanomaterials (Basel, Switzerland) · 2020Article
- Updated Insight into the Physiological and Pathological Roles of the Retromer Complex.International journal of molecular sciences · 2017Review
- Biogenesis of endosome-derived transport carriers.Cellular and molecular life sciences : CMLS · 2015Review
- Genome wide in silico analysis of Plasmodium falciparum phosphatome.BMC genomics · 2014Article
- The giardial VPS35 retromer subunit is necessary for multimeric complex assembly and interaction with the vacuolar protein sorting receptor.Biochimica et biophysica acta · 2013Article
- Phosphoinositides in the mammalian endo-lysosomal network.Sub-cellular biochemistry · 2012Review
- A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease.American journal of human genetics · 2011Article
- Evolutionary reconstruction of the retromer complex and its function in Trypanosoma brucei.Journal of cell science · 2011Article
- VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins.PloS one · 2011Article
- Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7.The Journal of cell biology · 2008Article
- Identification of a conserved motif required for Vps35p/Vps26p interaction and assembly of the retromer complex.The Biochemical journal · 2007Article
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The retromer complex is involved in the retrograde transport of the CI-M6PR (cation-independent mannose 6-phosphate receptor) from endosomes to the Golgi. It is a hetero-trimeric complex composed of Vps26 (vacuolar sorting protein 26), Vps29 and Vps35 proteins, which are conserved in eukaryote evolution. Recently, elucidation of the crystal structure of Vps29 revealed that Vps29 contains a metallo-phosphoesterase fold [Wang, Guo, Liang, Fan, Zhu, Zang, Zhu, Li, Teng, Niu et al. (2005) J. Biol. Chem. 280, 22962-22967; Collins, Skinner, Watson, Seaman and Owen (2005) Nat. Struct. Mol. Biol. 12, 594-602]. We demonstrate that recombinant hVps29 (human Vps29) displays in vitro phosphatase activity towards a serine-phosphorylated peptide, containing the acidic-cluster dileucine motif of the cytoplasmatic tail of the CI-M6PR. Efficient dephosphorylation required the additional presence of recombinant hVps26 and hVps35 proteins, which interact with hVps29. Phosphatase activity of hVps29 was greatly decreased by alanine substitutions of active-site residues that are predicted to co-ordinate metal ions. Using inductively coupled plasma MS, we demonstrate that recombinant hVps29 binds zinc. Moreover, hVps29-dependent phosphatase activity is greatly reduced by non-specific and zinc-specific metal ion chelators, which can be completely restored by addition of excess ZnCl2. The binuclear Zn2+ centre and phosphate group were modelled into the hVps29 catalytic site and pKa calculations provided further insight into the molecular mechanisms of Vps29 phosphatase activity. We conclude that the retromer complex displays Vps29-dependent in vitro phosphatase activity towards a serinephosphorylated acidic-cluster dileucine motif that is involved in endosomal trafficking of the CI-M6PR. The potential significance of these findings with respect to regulation of transport of cycling trans-Golgi network proteins is discussed.
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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.