The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Parkinson Disease-linked Vps35 R524W Mutation Impairs the Endosomal Association of Retromer and Induces α-Synuclein Aggregation
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The effect of R55 and R33 is primarily by restoring the function and localization of the retromer complex.
“It is now believed that the effect of R55 and R33 is primarily by restoring the function and localization of the retromer complex [10].”
From Stabilizing the retromer complex rescues synaptic dysfunction and endosomal trafficking deficits in an Alzheimer’s disease mouse model (2025) · cites this paper as [10]
The results on Vps35 mutant localization (Fig. 5) show that R55 increased endosomal localization and membrane recruitment of R524W-containing retromer, though it did not fully restore membrane levels. The Discussion suggests a possible mechanism for that effect, but our copy does not establish that restoring retromer function and localization is the primary mechanism of both agents; a search for R33 found no passage addressing it. (LLM, conf=0.86)
Experimental — accuracy not yet measuredDysfunctional retromer linked to neurodegenerative diseases is not primarily caused by loss of expression of Vps35 but by decreased endosomal association causing loss of function that can be mitigated by retromer stabilizing compounds such as R55 and R33.
“Our results supports previous reports that dysfunctional retromer linked to neurodegenerative diseases is not primarily caused by loss of expression of Vps35 but by decreased endosomal association causing loss of function that can be mitigated by retromer stabilizing compounds such as R55 and R33 [10].”
From Stabilizing the retromer complex rescues synaptic dysfunction and endosomal trafficking deficits in an Alzheimer’s disease mouse model (2025) · cites this paper as [10]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227
Lewy Body-like α-Synuclein Aggregates Resist Degradation and Impair Macroautophagy
Tanik, S. A., Schultheiss, C. E., Volpicelli-Daley, L. A., Brunden, K. R., & Lee, V. M. Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457408 · Cited by 326
Flagged first, then by citations
Research works printed but not linked: 51
- Xu, 2002, Dopamine-dependent neurotoxicity of α-synuclein: a mechanism for selective neurodegeneration in Parkinson disease, Nat. Med, 8, 600, 10.1038/nm0602-600 · DOI
- Emmanouilidou, 2010, Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome, Neurobiol. Aging, 31, 953, 10.1016/j.neurobiolaging.2008.07.008 · DOI
- Klein, 2012, Genetics of Parkinson's disease, Cold Spring Harb. Perspect. Med, 2, a008888, 10.1101/cshperspect.a008888 · DOI
- Zimprich, 2011, A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease, Am. J. Hum. Genet, 89, 168, 10.1016/j.ajhg.2011.06.008 · DOI · Paper page
- Lesage, 2012, Identification of VPS35 mutations replicated in French families with Parkinson disease, Neurology, 78, 1449, 10.1212/WNL.0b013e318253d5f2 · DOI
- MacLeod, 2013, RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk, Neuron, 77, 425, 10.1016/j.neuron.2012.11.033 · DOI · Paper page
- Haft, 2000, Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes, Mol. Biol. Cell, 11, 4105, 10.1091/mbc.11.12.4105 · DOI · Paper page
- Kerr, 2005, A novel mammalian retromer component, Vps26B, Traffic, 6, 991, 10.1111/j.1600-0854.2005.00328.x · DOI · Paper page
- Bugarcic, 2011, Vps26A and Vps26B subunits define distinct retromer complexes, Traffic, 12, 1759, 10.1111/j.1600-0854.2011.01284.x · DOI
- Arighi, 2004, Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor, J. Cell Biol, 165, 123, 10.1083/jcb.200312055 · DOI · Paper page
- Seaman, 2004, Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer, J. Cell Biol, 165, 111, 10.1083/jcb.200312034 · DOI · Paper page
- Seaman, 2007, Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval, J. Cell Sci, 120, 2378, 10.1242/jcs.009654 · DOI
- Seaman, 2012, The retromer complex: endosomal protein recycling and beyond, J. Cell Sci, 125, 4693
- Follett, 2016, Retromer's role in endosomal trafficking and impaired function in neurodegenerative diseases, Curr. Protein Pept. Sci
- Chi, 2015, Biogenesis of endosome-derived transport carriers, Cell. Mol. Life Sci, 72, 3441, 10.1007/s00018-015-1935-x · DOI
- Follett, 2014, The Vps35 D620N mutation linked to Parkinson's disease disrupts the cargo sorting function of retromer, Traffic, 15, 230, 10.1111/tra.12136 · DOI
- Munsie, 2015, Retromer-dependent neurotransmitter receptor trafficking to synapses is altered by the Parkinson's disease VPS35 mutation p.D620N, Hum. Mol. Genet, 24, 1691, 10.1093/hmg/ddu582 · DOI · Paper page
- McGough, 2014, Retromer binding to FAM21 and the WASH complex is perturbed by the Parkinson disease-linked VPS35(D620N) mutation, Curr. Biol, 24, 1670, 10.1016/j.cub.2014.06.024 · DOI · Paper page
- Gomez, 2009, A FAM21-containing WASH complex regulates retromer-dependent sorting, Dev. Cell, 17, 699, 10.1016/j.devcel.2009.09.009 · DOI · Paper page
- Zavodszky, 2014, Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy, Nat. Commun, 5, 3828, 10.1038/ncomms4828 · DOI · Paper page
- Hierro, 2007, Functional architecture of the retromer cargo-recognition complex, Nature, 449, 1063, 10.1038/nature06216 · DOI · Paper page
- Ariotti, 2015, Modular detection of GFP-labeled proteins for rapid screening by electron microscopy in cells and organisms, Dev. Cell, 35, 513, 10.1016/j.devcel.2015.10.016 · DOI
- Seaman, 2009, Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5, J. Cell Sci, 122, 2371, 10.1242/jcs.048686 · DOI · Paper page
- Harbour, 2010, The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics, J. Cell Sci, 123, 3703, 10.1242/jcs.071472 · DOI · Paper page
- Harbour, 2012, Recruitment of the endosomal WASH complex is mediated by the extended “tail” of Fam21 binding to the retromer protein Vps35, Biochem. J, 442, 209, 10.1042/BJ20111761 · DOI · Paper page
- Jia, 2012, Multiple repeat elements within the FAM21 tail link the WASH actin regulatory complex to the retromer, Mol. Biol. Cell, 23, 2352, 10.1091/mbc.e11-12-1059 · DOI · Paper page
- Mecozzi, 2014, Pharmacological chaperones stabilize retromer to limit APP processing, Nat. Chem. Biol, 10, 443, 10.1038/nchembio.1508 · DOI · Paper page
- Cullen, 2009, Cathepsin D expression level affects α-synuclein processing, aggregation, and toxicity in vivo, Mol. Brain, 2, 5, 10.1186/1756-6606-2-5 · DOI
- Follett, 2013, Potassium depolarization and raised calcium induces α-synuclein aggregates, Neurotox. Res, 23, 378, 10.1007/s12640-012-9366-z · DOI
- Decressac, 2013, TFEB-mediated autophagy rescues midbrain dopamine neurons from α-synuclein toxicity, Proc. Natl. Acad. Sci. U.S.A, 110, E1817, 10.1073/pnas.1305623110 · DOI · Paper page
- Konno, 2012, Suppression of dynamin GTPase decreases α-synuclein uptake by neuronal and oligodendroglial cells: a potent therapeutic target for synucleinopathy, Mol. Neurodegener, 7, 38, 10.1186/1750-1326-7-38 · DOI
- Temkin, 2011, SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors, Nat. Cell Biol, 13, 715, 10.1038/ncb2252 · DOI · Paper page
- Steinberg, 2013, A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport, Nat. Cell Biol, 15, 461, 10.1038/ncb2721 · DOI · Paper page
- Gallon, 2014, A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer, Proc. Natl. Acad. Sci. U.S.A, 111, E3604, 10.1073/pnas.1410552111 · DOI · Paper page
- Popovic, 2012, Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers, Mol. Cell. Biol, 32, 1733, 10.1128/MCB.06717-11 · DOI
- Hong, 2009, The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport, Cell Res, 19, 1334, 10.1038/cr.2009.130 · DOI
- Harrison, 2014, A mechanism for retromer endosomal coat complex assembly with cargo, Proc. Natl. Acad. Sci. U.S.A, 111, 267, 10.1073/pnas.1316482111 · DOI
- Priya, 2015, Molecular insights into Rab7-mediated endosomal recruitment of core retromer: deciphering the role of Vps26 and Vps35, Traffic, 16, 68, 10.1111/tra.12237 · DOI
- Hossain, 2001, Limited proteolysis of NACP/α-synuclein, J. Alzheimers Dis, 3, 577, 10.3233/JAD-2001-3608 · DOI
- Sevlever, 2008, Cathepsin D is the main lysosomal enzyme involved in the degradation of α-synuclein and generation of its carboxy-terminally truncated species, Biochemistry, 47, 9678, 10.1021/bi800699v · DOI · Paper page
- Miura, 2014, VPS35 dysfunction impairs lysosomal degradation of α-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease, Neurobiol. Dis, 71, 1, 10.1016/j.nbd.2014.07.014 · DOI
- Cuervo, 2000, Age-related decline in chaperone-mediated autophagy, J. Biol. Chem, 275, 31505, 10.1074/jbc.M002102200 · DOI · Paper page
- Li, 2003, Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production, J. Biol. Chem, 278, 8516, 10.1074/jbc.M210432200 · DOI
- Yoshimori, 1991, Bafilomycin A1, a specific inhibitor of vacuolar-type H+-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells, J. Biol. Chem, 266, 17707, 10.1016/S0021-9258(19)47429-2 · DOI
- Jäger, 2004, Role for Rab7 in maturation of late autophagic vacuoles, J. Cell Sci, 117, 4837, 10.1242/jcs.01370 · DOI
- Popovic, 2014, TBC1D5 and the AP2 complex regulate ATG9 trafficking and initiation of autophagy, EMBO Rep, 15, 392, 10.1002/embr.201337995 · DOI
- Rojas, 2008, Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7, J. Cell Biol, 183, 513, 10.1083/jcb.200804048 · DOI · Paper page
- Norwood, 2011, Assembly and solution structure of the core retromer protein complex, Traffic, 12, 56, 10.1111/j.1600-0854.2010.01124.x · DOI · Paper page
- Furlong, 2000, α-Synuclein overexpression promotes aggregation of mutant huntingtin, Biochem. J, 346, 577, 10.1042/bj3460577 · DOI
- Lee, 2002, Formation and removal of α-synuclein aggregates in cells exposed to mitochondrial inhibitors, J. Biol. Chem, 277, 5411, 10.1074/jbc.M105326200 · DOI
- Scotter, 2014, Differential roles of the ubiquitin proteasome system and autophagy in the clearance of soluble and aggregated TDP-43 species, J. Cell Sci, 127, 1263
Cited by
Sorted by citations
The Retromer Complex: From Genesis to Revelations
Seaman, M. N. J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.12.009 · Cited by 104
Receptor Recycling by Retromer
Carosi, J. M., Denton, D., Kumar, S., & Sargeant, T. J. (2023) · Molecular and Cellular Biology · doi:10.1080/10985549.2023.2222053 · Cited by 36
Manecka, D.-L., Vanderperre, B., Fon, E. A., & Durcan, T. M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00311 · Cited by 21
Retromer dysfunction at the nexus of tauopathies
Carosi, J. M., Denton, D., Kumar, S., & Sargeant, T. J. (2021) · Cell Death & Differentiation · doi:10.1038/s41418-020-00727-2 · Cited by 16
Ramonet, D., Daerr, A., & Hallbeck, M. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02096-8 · Cited by 7
Metadata
- Authors
- Follett, J., Bugarcic, A., Yang, Z., Ariotti, N., Norwood, S. J., Collins, B. M., Parton, R. G., & Teasdale, R. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-08
- Volume
- 291
- Issue
- 35
- Pages
- 18283-18298
- ISSN
- 0021-9258
- Cited by
- 81
- References
- 3
- Language
- en
- Licence
- Funders
- National Health and Medical Research Council (APP1025538, APP1042082, APP1058734, APP1041929, APP1061574, APP1045092, APP1037320, APP1058565)
- Australian Research Council (DP120103930, FT100100027)
- Judith Jane Mason and Harold Stannett Williams Memorial Foundation
- Australian Cancer Research Foundation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review