Vacuolar protein sorting-associated protein 29 (VPS29) is a catalytically inactive metallophosphoesterase-fold scaffolding subunit shared between two endosomal cargo-coat complexes: the heterotrimeric retromer cargo-selective complex (VPS35-VPS26-VPS29) and the retriever complex (VPS35L-VPS26C-VPS29, part of Commander). Bound in a C-terminal alpha-helical solenoid cradle of VPS35 (or VPS35L), VPS29 presents a conserved hydrophobic surface (centered on Leu152) that recruits regulatory cofactors including the Rab7 GTPase-activating protein TBC1D5 and the VARP adaptor, supporting both endosome-to-Golgi retrograde retrieval and endosome-to-plasma-membrane recycling.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:11102511 Human orthologs of yeast vacuolar protein sorting proteins V... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:11102511 Human orthologs of yeast vacuolar protein sorting proteins V... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:16732284 The retromer subunit Vps26 has an arrestin fold and binds Vp... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:17891154 Functional architecture of the retromer cargo-recognition co... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:17891154 Functional architecture of the retromer cargo-recognition co... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:19619496 The retromer coat complex coordinates endosomal sorting and ... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:19619496 The retromer coat complex coordinates endosomal sorting and ... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:20923837 The cargo-selective retromer complex is a recruiting hub for... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:24152121 The Vps35 D620N mutation linked to Parkinson's disease disru... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:24344282 A mechanism for retromer endosomal coat complex assembly wit... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:24344282 A mechanism for retromer endosomal coat complex assembly wit... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:24603492 TBC1D5 and the AP2 complex regulate ATG9 trafficking and ini... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:24747528 Pharmacological chaperones stabilize retromer to limit APP p... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:24980502 Retromer binding to FAM21 and the WASH complex is perturbed ... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:25502805 A massively parallel pipeline to clone DNA variants and exam... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:27385586 Parkinson Disease-linked Vps35 R524W Mutation Impairs the En... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:27385586 Parkinson Disease-linked Vps35 R524W Mutation Impairs the En... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:28892079 Retriever is a multiprotein complex for retromer-independent... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:28892079 Retriever is a multiprotein complex for retromer-independent... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:37172566 Structure of the endosomal Commander complex linked to Ritsc... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:37172566 Structure of the endosomal Commander complex linked to Ritsc... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:37172566 Structure of the endosomal Commander complex linked to Ritsc... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:37172566 Structure of the endosomal Commander complex linked to Ritsc... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Uninformative generic protein binding term removed per policy. Reason: Broad GO:0005515 protein binding annotation is removed as uninformative per the protein-binding policy; VPS29's assembly into retromer/retriever complexes and cooperative cargo adaptor role are captured by GO:0030906 and GO:0140312. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: Cytoplasm localization is true but too general; refine to cytosol and endosome membrane. Reason: VPS29 partitions between a soluble cytosolic pool and the cytoplasmic surface of endosomal membranes within retromer and retriever complexes; refine GO:0005737 (cytoplasm) to GO:0005829 (cytosol) and GO:0010008 (endosome membrane). Proposed replacements: cytosol endosome membrane Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. PMID:15078903 In particular, retromer is associated with tubular-vesicular profiles that emanate from early endosomes or from intermediates in the maturation from early to late endosomes. |
| GO:0005768 endosome | IBA GO_REF:0000033 | ACCEPT | Summary: VPS29 localizes to and functions at endosomes as part of retromer and retriever. Reason: Direct localization and functional studies demonstrate that VPS29 is recruited to endosomes as an integral subunit of both the retromer and retriever cargo-sorting complexes. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000122547 · VPS29 clade node SUPPORTS TRANSFER Conserved eukaryotic VPS29 subfamily node. SGD:S000001054 · yeast VPS29 SUPPORTS TRANSFER Foundational yeast retromer Vps29 subunit. UniProtKB:Q9UBQ0 · human VPS29 SUPPORTS TRANSFER Direct experimental evidence in human. Supporting Evidence: PMID:15078903 In particular, retromer is associated with tubular-vesicular profiles that emanate from early endosomes or from intermediates in the maturation from early to late endosomes. PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. |
| GO:0005768 endosome | IDA GO_REF:0000054 | ACCEPT | Summary: VPS29 localizes to and functions at endosomes as part of retromer and retriever. Reason: Direct localization and functional studies demonstrate that VPS29 is recruited to endosomes as an integral subunit of both the retromer and retriever cargo-sorting complexes. Supporting Evidence: PMID:15078903 In particular, retromer is associated with tubular-vesicular profiles that emanate from early endosomes or from intermediates in the maturation from early to late endosomes. PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. |
| GO:0005768 endosome | IEA GO_REF:0000117 | ACCEPT | Summary: VPS29 localizes to and functions at endosomes as part of retromer and retriever. Reason: Direct localization and functional studies demonstrate that VPS29 is recruited to endosomes as an integral subunit of both the retromer and retriever cargo-sorting complexes. Supporting Evidence: PMID:15078903 In particular, retromer is associated with tubular-vesicular profiles that emanate from early endosomes or from intermediates in the maturation from early to late endosomes. PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. |
| GO:0005769 early endosome | IEA GO_REF:0000044 | ACCEPT | Summary: VPS29 localizes to early endosomes where retromer and retriever sort cargo. Reason: Immunofluorescence and immunoelectron microscopy show that human VPS29 localizes to early endosomes and their tubular exit domains. Supporting Evidence: PMID:15078903 In particular, retromer is associated with tubular-vesicular profiles that emanate from early endosomes or from intermediates in the maturation from early to late endosomes. |
| GO:0005770 late endosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retromer remains associated with maturing early-to-late endosomes during Rab7 recruitment. Reason: VPS29-containing retromer complexes associate with Rab7 and TBC1D5 on maturing/late endosomal membranes, peripheral to the primary sorting station on early/tubular endosomes. Supporting Evidence: PMID:15078903 In particular, retromer is associated with tubular-vesicular profiles that emanate from early endosomes or from intermediates in the maturation from early to late endosomes. file:human/VPS29/VPS29-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Endosome membrane {ECO:0000250|UniProtKB:Q9QZ88}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QZ88}. Early endosome {ECO:0000305}. Late endosome {ECO:0000305}. |
| GO:0005789 endoplasmic reticulum membrane | NAS PMID:34943955 Commander Complex-A Multifaceted Operator in Intracellular S... | REMOVE | Summary: Spurious NAS annotation to endoplasmic reticulum membrane from an endosomal Commander review article. Reason: PMID:34943955 is a review of endosomal cargo retrieval by the Commander/retriever complex; VPS29 localizes to the cytosol and endosomal membranes (GO:0010008), not the endoplasmic reticulum membrane (GO:0005789). Supporting Evidence: PMID:34943955 Commander complex is a 16-protein complex that plays multiple roles in various intracellular events in endosomal cargo and in the regulation of cell homeostasis, cell cycle and immune response. It consists of COMMD1-10, CCDC22, CCDC93, DENND10, VPS26C, VPS29, and VPS35L. file:human/VPS29/VPS29-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Endosome membrane {ECO:0000250|UniProtKB:Q9QZ88}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QZ88}. Early endosome {ECO:0000305}. Late endosome {ECO:0000305}. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: VPS29 exists in a soluble cytosolic pool in equilibrium with endosome-bound retromer and retriever. Reason: Biochemical fractionation and imaging demonstrate that VPS29 is present in the cytosol as part of soluble retromer/retriever heterotrimers that cycle onto endosomal membranes. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. |
| GO:0005829 cytosol | IDA PMID:11102511 Human orthologs of yeast vacuolar protein sorting proteins V... | ACCEPT | Summary: VPS29 exists in a soluble cytosolic pool in equilibrium with endosome-bound retromer and retriever. Reason: Biochemical fractionation and imaging demonstrate that VPS29 is present in the cytosol as part of soluble retromer/retriever heterotrimers that cycle onto endosomal membranes. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3247836 | ACCEPT | Summary: VPS29 exists in a soluble cytosolic pool in equilibrium with endosome-bound retromer and retriever. Reason: Biochemical fractionation and imaging demonstrate that VPS29 is present in the cytosol as part of soluble retromer/retriever heterotrimers that cycle onto endosomal membranes. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3247839 | ACCEPT | Summary: VPS29 exists in a soluble cytosolic pool in equilibrium with endosome-bound retromer and retriever. Reason: Biochemical fractionation and imaging demonstrate that VPS29 is present in the cytosol as part of soluble retromer/retriever heterotrimers that cycle onto endosomal membranes. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3247849 | ACCEPT | Summary: VPS29 exists in a soluble cytosolic pool in equilibrium with endosome-bound retromer and retriever. Reason: Biochemical fractionation and imaging demonstrate that VPS29 is present in the cytosol as part of soluble retromer/retriever heterotrimers that cycle onto endosomal membranes. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. |
| GO:0010008 endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: VPS29 associates with the cytoplasmic surface of the endosome membrane. Reason: VPS29 is recruited to the endosome membrane as an essential subunit of both retromer and retriever complexes. Supporting Evidence: PMID:30072228 Retromer, an ancient multi-protein complex, is essential for the retrieval and recycling of hundreds of transmembrane proteins. PMID:34943955 Commander complex is a 16-protein complex that plays multiple roles in various intracellular events in endosomal cargo and in the regulation of cell homeostasis, cell cycle and immune response. It consists of COMMD1-10, CCDC22, CCDC93, DENND10, VPS26C, VPS29, and VPS35L. |
| GO:0010008 endosome membrane | ISS GO_REF:0000024 | ACCEPT | Summary: VPS29 associates with the cytoplasmic surface of the endosome membrane. Reason: VPS29 is recruited to the endosome membrane as an essential subunit of both retromer and retriever complexes. Supporting Evidence: PMID:30072228 Retromer, an ancient multi-protein complex, is essential for the retrieval and recycling of hundreds of transmembrane proteins. PMID:34943955 Commander complex is a 16-protein complex that plays multiple roles in various intracellular events in endosomal cargo and in the regulation of cell homeostasis, cell cycle and immune response. It consists of COMMD1-10, CCDC22, CCDC93, DENND10, VPS26C, VPS29, and VPS35L. |
| GO:0010008 endosome membrane | NAS PMID:30072228 Endosomal Retrieval of Cargo: Retromer Is Not Alone. | ACCEPT | Summary: VPS29 associates with the cytoplasmic surface of the endosome membrane. Reason: VPS29 is recruited to the endosome membrane as an essential subunit of both retromer and retriever complexes. Supporting Evidence: PMID:30072228 Retromer, an ancient multi-protein complex, is essential for the retrieval and recycling of hundreds of transmembrane proteins. PMID:34943955 Commander complex is a 16-protein complex that plays multiple roles in various intracellular events in endosomal cargo and in the regulation of cell homeostasis, cell cycle and immune response. It consists of COMMD1-10, CCDC22, CCDC93, DENND10, VPS26C, VPS29, and VPS35L. |
| GO:0010008 endosome membrane | NAS PMID:34943955 Commander Complex-A Multifaceted Operator in Intracellular S... | ACCEPT | Summary: VPS29 associates with the cytoplasmic surface of the endosome membrane. Reason: VPS29 is recruited to the endosome membrane as an essential subunit of both retromer and retriever complexes. Supporting Evidence: PMID:30072228 Retromer, an ancient multi-protein complex, is essential for the retrieval and recycling of hundreds of transmembrane proteins. PMID:34943955 Commander complex is a 16-protein complex that plays multiple roles in various intracellular events in endosomal cargo and in the regulation of cell homeostasis, cell cycle and immune response. It consists of COMMD1-10, CCDC22, CCDC93, DENND10, VPS26C, VPS29, and VPS35L. |
| GO:0010506 regulation of autophagy | IMP NOT PMID:24603492 TBC1D5 and the AP2 complex regulate ATG9 trafficking and ini... | ACCEPT | Summary: Curated NOT|involved_in annotation from PMID:24603492, which shows that TBC1D5 and the AP2 complex regulate ATG9 trafficking toward autophagosome formation. Reason: This row carries a curated NOT|involved_in qualifier from PMID:24603492; while TBC1D5 binds VPS29 on endosomes, PMID:24603492 establishes that TBC1D5 and the clathrin adaptor AP2 complex regulate the rerouting of ATG9-containing vesicular carriers toward sites of autophagosome formation via ATG9 and the active ULK1 complex, supporting retention of the curator's negative assertion on VPS29. Supporting Evidence: PMID:24603492 The RabGAP protein TBC1D5 controls cellular endomembrane trafficking processes and binds the retromer subunit VPS29 and the ubiquitin-like protein ATG8 (LC3). Here, we describe that TBC1D5 also associates with ATG9 and the active ULK1 complex during autophagy. Moreover, ATG9 and TBC1D5 interact with clathrin and the AP2 complex. ... Taken together, our data show that TBC1D5 and the AP2 complex are important novel regulators of the rerouting of ATG9-containing vesicular carriers toward sites of autophagosome formation. |
| GO:0016020 membrane | IEA GO_REF:0000044 | MODIFY | Summary: Generic membrane term should be refined to endosome membrane. Reason: GO:0016020 (membrane) is too general; VPS29 specifically associates with the cytoplasmic face of the endosome membrane (GO:0010008). Proposed replacements: endosome membrane Supporting Evidence: PMID:30072228 Retromer, an ancient multi-protein complex, is essential for the retrieval and recycling of hundreds of transmembrane proteins. |
| GO:0030904 retromer complex | IBA GO_REF:0000033 | ACCEPT | Summary: VPS29 is an essential subunit of the retromer complex. Reason: Biochemical and structural analyses demonstrate that VPS29 binds the C-terminal alpha-helical solenoid of VPS35 as an integral subunit of the retromer complex. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000122547 · VPS29 clade node SUPPORTS TRANSFER Conserved eukaryotic VPS29 subfamily node. SGD:S000001054 · yeast VPS29 SUPPORTS TRANSFER Foundational yeast retromer Vps29 subunit. UniProtKB:Q9UBQ0 · human VPS29 SUPPORTS TRANSFER Direct experimental evidence in human. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. PMID:17891154 Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. |
| GO:0030904 retromer complex | IDA PMID:11102511 Human orthologs of yeast vacuolar protein sorting proteins V... | ACCEPT | Summary: VPS29 is an essential subunit of the retromer complex. Reason: Biochemical and structural analyses demonstrate that VPS29 binds the C-terminal alpha-helical solenoid of VPS35 as an integral subunit of the retromer complex. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. PMID:17891154 Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. |
| GO:0030904 retromer complex | IDA PMID:28892079 Retriever is a multiprotein complex for retromer-independent... | ACCEPT | Summary: VPS29 is an essential subunit of the retromer complex. Reason: Biochemical and structural analyses demonstrate that VPS29 binds the C-terminal alpha-helical solenoid of VPS35 as an integral subunit of the retromer complex. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. PMID:17891154 Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. |
| GO:0030904 retromer complex | IEA GO_REF:0000120 | ACCEPT | Summary: VPS29 is an essential subunit of the retromer complex. Reason: Biochemical and structural analyses demonstrate that VPS29 binds the C-terminal alpha-helical solenoid of VPS35 as an integral subunit of the retromer complex. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. PMID:17891154 Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. |
| GO:0030906 retromer, cargo-selective complex | IDA PMID:27385586 Parkinson Disease-linked Vps35 R524W Mutation Impairs the En... | ACCEPT | Summary: VPS29 is a core subunit of the heterotrimeric retromer cargo-selective complex (VPS35-VPS26-VPS29). Reason: Crystal structures and reconstitution studies confirm that VPS29 forms the heterotrimeric retromer cargo-selective complex with VPS35 and VPS26A/B. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. PMID:17891154 Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. PMID:27385586 Retromer is a heterotrimeric complex that associates with endosomal membranes and facilitates the retrograde sorting of multiple receptors, including the cation-independent mannose 6-phosphate receptor for lysosomal enzymes. PMID:26220253 Retrograde transport from the endosome to the Golgi is mediated by a 5 protein complex known as the retromer. |
| GO:0030906 retromer, cargo-selective complex | IPI PMID:11102511 Human orthologs of yeast vacuolar protein sorting proteins V... | ACCEPT | Summary: VPS29 is a core subunit of the heterotrimeric retromer cargo-selective complex (VPS35-VPS26-VPS29). Reason: Crystal structures and reconstitution studies confirm that VPS29 forms the heterotrimeric retromer cargo-selective complex with VPS35 and VPS26A/B. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. PMID:17891154 Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. PMID:27385586 Retromer is a heterotrimeric complex that associates with endosomal membranes and facilitates the retrograde sorting of multiple receptors, including the cation-independent mannose 6-phosphate receptor for lysosomal enzymes. PMID:26220253 Retrograde transport from the endosome to the Golgi is mediated by a 5 protein complex known as the retromer. |
| GO:0030906 retromer, cargo-selective complex | NAS PMID:26220253 Retromer: Structure, function, and roles in mammalian diseas... | ACCEPT | Summary: VPS29 is a core subunit of the heterotrimeric retromer cargo-selective complex (VPS35-VPS26-VPS29). Reason: Crystal structures and reconstitution studies confirm that VPS29 forms the heterotrimeric retromer cargo-selective complex with VPS35 and VPS26A/B. Supporting Evidence: PMID:11102511 We report the cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. ... Furthermore, hVps35, hVps29, and hVps26 have been found in membrane-associated and cytosolic compartments. PMID:17891154 Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. PMID:27385586 Retromer is a heterotrimeric complex that associates with endosomal membranes and facilitates the retrograde sorting of multiple receptors, including the cation-independent mannose 6-phosphate receptor for lysosomal enzymes. PMID:26220253 Retrograde transport from the endosome to the Golgi is mediated by a 5 protein complex known as the retromer. |
| GO:0032456 endocytic recycling | IMP PMID:28892079 Retriever is a multiprotein complex for retromer-independent... | ACCEPT | Summary: VPS29 is required for endocytic recycling of transmembrane cargoes to the plasma membrane via both SNX27-retromer and SNX17-retriever. Reason: As a shared subunit of both retromer and retriever (VPS35L-VPS26C-VPS29), VPS29 is essential for endosome-to-plasma-membrane recycling of hundreds of receptors, integrins, and solute carriers. Supporting Evidence: PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. PMID:30072228 Retromer, an ancient multi-protein complex, is essential for the retrieval and recycling of hundreds of transmembrane proteins. PMID:34943955 Commander complex is a 16-protein complex that plays multiple roles in various intracellular events in endosomal cargo and in the regulation of cell homeostasis, cell cycle and immune response. It consists of COMMD1-10, CCDC22, CCDC93, DENND10, VPS26C, VPS29, and VPS35L. |
| GO:0032456 endocytic recycling | NAS PMID:30072228 Endosomal Retrieval of Cargo: Retromer Is Not Alone. | ACCEPT | Summary: VPS29 is required for endocytic recycling of transmembrane cargoes to the plasma membrane via both SNX27-retromer and SNX17-retriever. Reason: As a shared subunit of both retromer and retriever (VPS35L-VPS26C-VPS29), VPS29 is essential for endosome-to-plasma-membrane recycling of hundreds of receptors, integrins, and solute carriers. Supporting Evidence: PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. PMID:30072228 Retromer, an ancient multi-protein complex, is essential for the retrieval and recycling of hundreds of transmembrane proteins. PMID:34943955 Commander complex is a 16-protein complex that plays multiple roles in various intracellular events in endosomal cargo and in the regulation of cell homeostasis, cell cycle and immune response. It consists of COMMD1-10, CCDC22, CCDC93, DENND10, VPS26C, VPS29, and VPS35L. |
| GO:0032456 endocytic recycling | NAS PMID:34943955 Commander Complex-A Multifaceted Operator in Intracellular S... | ACCEPT | Summary: VPS29 is required for endocytic recycling of transmembrane cargoes to the plasma membrane via both SNX27-retromer and SNX17-retriever. Reason: As a shared subunit of both retromer and retriever (VPS35L-VPS26C-VPS29), VPS29 is essential for endosome-to-plasma-membrane recycling of hundreds of receptors, integrins, and solute carriers. Supporting Evidence: PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. PMID:30072228 Retromer, an ancient multi-protein complex, is essential for the retrieval and recycling of hundreds of transmembrane proteins. PMID:34943955 Commander complex is a 16-protein complex that plays multiple roles in various intracellular events in endosomal cargo and in the regulation of cell homeostasis, cell cycle and immune response. It consists of COMMD1-10, CCDC22, CCDC93, DENND10, VPS26C, VPS29, and VPS35L. |
| GO:0032991 protein-containing complex | IDA PMID:28892079 Retriever is a multiprotein complex for retromer-independent... | MODIFY | Summary: Root protein-containing complex term from Retriever/Commander papers should be refined to commander complex. Reason: PMID:28892079 and PMID:37172566 demonstrate that VPS29 is an integral subunit of the Retriever heterotrimer (VPS35L-VPS26C-VPS29) within the Commander complex; root GO:0032991 is refined to GO:0160309 (commander complex). Proposed replacements: commander complex Supporting Evidence: PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. PMID:37172566 It comprises two sub-assemblies: Retriever composed of VPS35L, VPS26C, and VPS29; and the CCC complex which contains twelve subunits: COMMD1-COMMD10 and the coiled-coil domain-containing (CCDC) proteins CCDC22 and CCDC93. |
| GO:0032991 protein-containing complex | IDA PMID:37172566 Structure of the endosomal Commander complex linked to Ritsc... | MODIFY | Summary: Root protein-containing complex term from Retriever/Commander papers should be refined to commander complex. Reason: PMID:28892079 and PMID:37172566 demonstrate that VPS29 is an integral subunit of the Retriever heterotrimer (VPS35L-VPS26C-VPS29) within the Commander complex; root GO:0032991 is refined to GO:0160309 (commander complex). Proposed replacements: commander complex Supporting Evidence: PMID:28892079 We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. PMID:37172566 It comprises two sub-assemblies: Retriever composed of VPS35L, VPS26C, and VPS29; and the CCC complex which contains twelve subunits: COMMD1-COMMD10 and the coiled-coil domain-containing (CCDC) proteins CCDC22 and CCDC93. |
| GO:0042147 retrograde transport, endosome to Golgi | IBA GO_REF:0000033 | ACCEPT | Summary: VPS29 is required within the retromer complex for retrograde transport from endosomes to the trans-Golgi network. Reason: Depletion of VPS29 disrupts retromer stability and impairs retrograde retrieval of CI-MPR and other cargoes from endosomes to the Golgi. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000122547 · VPS29 clade node SUPPORTS TRANSFER Conserved eukaryotic VPS29 subfamily node. SGD:S000001054 · yeast VPS29 SUPPORTS TRANSFER Foundational yeast retromer Vps29 subunit. Supporting Evidence: PMID:15078903 Depletion of retromer by RNA interference increases the lysosomal turnover of the CI-MPR, decreases cellular levels of lysosomal hydrolases, and causes swelling of lysosomes. PMID:26220253 Retrograde transport from the endosome to the Golgi is mediated by a 5 protein complex known as the retromer. |
| GO:0042147 retrograde transport, endosome to Golgi | IEA GO_REF:0000002 | ACCEPT | Summary: VPS29 is required within the retromer complex for retrograde transport from endosomes to the trans-Golgi network. Reason: Depletion of VPS29 disrupts retromer stability and impairs retrograde retrieval of CI-MPR and other cargoes from endosomes to the Golgi. Supporting Evidence: PMID:15078903 Depletion of retromer by RNA interference increases the lysosomal turnover of the CI-MPR, decreases cellular levels of lysosomal hydrolases, and causes swelling of lysosomes. PMID:26220253 Retrograde transport from the endosome to the Golgi is mediated by a 5 protein complex known as the retromer. |
| GO:0042147 retrograde transport, endosome to Golgi | NAS PMID:26220253 Retromer: Structure, function, and roles in mammalian diseas... | ACCEPT | Summary: VPS29 is required within the retromer complex for retrograde transport from endosomes to the trans-Golgi network. Reason: Depletion of VPS29 disrupts retromer stability and impairs retrograde retrieval of CI-MPR and other cargoes from endosomes to the Golgi. Supporting Evidence: PMID:15078903 Depletion of retromer by RNA interference increases the lysosomal turnover of the CI-MPR, decreases cellular levels of lysosomal hydrolases, and causes swelling of lysosomes. PMID:26220253 Retrograde transport from the endosome to the Golgi is mediated by a 5 protein complex known as the retromer. |
| GO:0140312 cargo adaptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: VPS29 contributes to cargo adaptor activity as an integral subunit of the retromer and retriever complexes. Reason: Within the heterotrimeric retromer CSC (and retriever), VPS29 stabilizes the C-terminal solenoid of VPS35, promotes helical coat oligomerization, and recruits TBC1D5/VARP to coordinate endosomal cargo adaptor activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000122547 · VPS29 clade node SUPPORTS TRANSFER Placed on the VPS29 subfamily clade (PTHR11124:SF12), excluding divergent metallophosphoesterases outside SF12. SGD:S000001054 · yeast VPS29 SUPPORTS TRANSFER Canonical yeast retromer subunit. Supporting Evidence: PMID:17891154 Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. PMID:27385586 Retromer is a heterotrimeric complex that associates with endosomal membranes and facilitates the retrograde sorting of multiple receptors, including the cation-independent mannose 6-phosphate receptor for lysosomal enzymes. |
| GO:0097422 tubular endosome | IDA PMID:15078903 Role of the mammalian retromer in sorting of the cation-inde... | NEW | Summary: VPS29 localizes to tubular domains of early endosomes together with VPS26 and VPS35. Reason: Direct immunofluorescence microscopy in PMID:15078903 demonstrates that human Vps29 (together with Vps26 and Vps35) localizes to the tubular domains of early endosomes where CI-MPR is enriched prior to transport to the TGN, providing direct experimental sub-compartment evidence beyond the root early endosome membrane term (GO:0031901). Supporting Evidence: PMID:15078903 In particular, retromer is associated with tubular-vesicular profiles that emanate from early endosomes or from intermediates in the maturation from early to late endosomes. |
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Download this section (compressed HTML)Q: What cellular mechanisms partition the shared VPS29 subunit pool between VPS35 (retromer) and VPS35L (retriever), and how does competition for the VPS29 Leu152 hydrophobic pocket among TBC1D5, VARP, and Commander subunits regulate endosomal tubule fission?
Experiment: Measure competitive binding kinetics of TBC1D5, VARP, and CCC complex subunits to VPS29 assembled in purified retromer vs retriever heterotrimers using surface plasmon resonance and cryo-EM.
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