| Potential functions and causal associations of VPS29 in hepatocellular carcinoma: a bioinformatic and Mendelian randomization study. | Potential functions and causal associations of VPS29 in hepatocellular carcinoma: a bioinformatic and Mendelian randomization study.
Yao YQ, Lv JL. | 11/7/2023 |
| Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29. | Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29.
Crawley-Snowdon H, Yang JC, Zaccai NR, Davis LJ, Wartosch L, Herman EK, Bright NA, Swarbrick JS, Collins BM, Jackson LP, Seaman MNJ, Luzio JP, Dacks JB, Neuhaus D, Owen DJ., Free PMC Article | 10/31/2020 |
| Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis. | Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis.
Muzio L, Sirtori R, Gornati D, Eleuteri S, Fossaghi A, Brancaccio D, Manzoni L, Ottoboni L, Feo L, Quattrini A, Mastrangelo E, Sorrentino L, Scalone E, Comi G, Marinelli L, Riva N, Milani M, Seneci P, Martino G., Free PMC Article | 09/12/2020 |
| RidL is critical for binding of the L. pneumophila effector to the Vps29 retromer subunit and displacement of the regulator TBC1D5. | Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5.
Bärlocher K, Hutter CAJ, Swart AL, Steiner B, Welin A, Hohl M, Letourneur F, Seeger MA, Hilbi H., Free PMC Article | 09/29/2018 |
| The retromer complex is a highly conserved membrane trafficking assembly composed of three proteins - Vps26, Vps29 and Vps35, which are impaired in neurodegenerative diseases. (Review) | Retromer's Role in Endosomal Trafficking and Impaired Function in Neurodegenerative Diseases.
Follett J, Bugarcic A, Collins BM, Teasdale RD. | 11/4/2017 |
| Heterotrimer composed of DSCR3, C16orf62 and VPS29 orchestrates endosomal cargo retrieval and recycling. | Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling.
McNally KE, Faulkner R, Steinberg F, Gallon M, Ghai R, Pim D, Langton P, Pearson N, Danson CM, Nägele H, Morris LL, Singla A, Overlee BL, Heesom KJ, Sessions R, Banks L, Collins BM, Berger I, Billadeau DD, Burstein E, Cullen PJ., Free PMC Article | 10/28/2017 |
| This study demonstrated that Genetic variability of VPS29 in parkinsonism. | Genetic variability of the retromer cargo recognition complex in parkinsonism.
Gustavsson EK, Guella I, Trinh J, Szu-Tu C, Rajput A, Rajput AH, Steele JC, McKeown M, Jeon BS, Aasly JO, Farrer MJ. | 12/26/2015 |
| Data indicate that vesicular transport proteins VPS35 and VPS29 influence the levels of the other subunit of retromer. | VPS29-VPS35 intermediate of retromer is stable and may be involved in the retromer complex assembly process.
Fuse A, Furuya N, Kakuta S, Inose A, Sato M, Koike M, Saiki S, Hattori N. | 08/8/2015 |
| Mutations in the gene composing the retromer cargo recognition subunit are not a common cause of Parkinson's disease. | Genetic variation of the retromer subunits VPS26A/B-VPS29 in Parkinson's disease.
Shannon B, Soto-Ortolaza A, Rayaprolu S, Cannon HD, Labbé C, Benitez BA, Choi J, Lynch T, Boczarska-Jedynak M, Opala G, Krygowska-Wajs A, Barcikowska M, Van Gerpen JA, Uitti RJ, Springer W, Cruchaga C, Wszolek ZK, Ross OA., Free PMC Article | 12/20/2014 |
| 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. | VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins.
Swarbrick JD, Shaw DJ, Chhabra S, Ghai R, Valkov E, Norwood SJ, Seaman MN, Collins BM., Free PMC Article | 09/24/2011 |
| Membrane recruitment of the cargo-selective retromer subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5. | Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5.
Seaman MN, Harbour ME, Tattersall D, Read E, Bright N., Free PMC Article | 01/21/2010 |
| crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 acts as a scaffold for the carboxy-terminal half of VPS35 | Functional architecture of the retromer cargo-recognition complex.
Hierro A, Rojas AL, Rojas R, Murthy N, Effantin G, Kajava AV, Steven AC, Bonifacino JS, Hurley JH., Free PMC Article | 01/21/2010 |
| These observations indicate that the mammalian retromer complex assembles by sequential association of SNX1/2 and Vps26-Vps29-Vps35 subcomplexes on endosomal membranes and that SNX1 and SNX2 play interchangeable but essential roles. | Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors.
Rojas R, Kametaka S, Haft CR, Bonifacino JS., Free PMC Article | 01/21/2010 |
| analysis of the phosphodiesterase/nuclease-like fold and two protein-protein interaction sites in human VPS29 | Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites.
Wang D, Guo M, Liang Z, Fan J, Zhu Z, Zang J, Zhu Z, Li X, Teng M, Niu L, Dong Y, Liu P. | 01/21/2010 |
| It was demonstrated that recombinant 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. | The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide.
Damen E, Krieger E, Nielsen JE, Eygensteyn J, van Leeuwen JE., Free PMC Article | 01/21/2010 |