{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T21:56:37Z","timestamp":1790718997248,"version":"4.1.0"},"reference-count":164,"publisher":"Portland Press Ltd.","issue":"13","license":[{"start":{"date-parts":[[2025,6,26]],"date-time":"2025-06-26T00:00:00Z","timestamp":1750896000000},"content-version":"vor","delay-in-days":1,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2025,7,2]]},"abstract":"<jats:p>Axonal transport is crucial for neuronal health and function, facilitating the delivery of newly synthesized material from the soma via anterograde transport and the removal of aged proteins and damaged organelles for degradation via retrograde transport. Emerging evidence links Parkinson\u2019s disease (PD)-causing mutations in the leucine-rich repeat kinase 2 (LRRK2) gene to dysfunctional axonal transport. Pathogenic LRRK2 mutations induce increased LRRK2 kinase activity, leading to the hyperphosphorylation of RAB proteins, which are key regulators of intracellular trafficking and transport. Here, we review the current literature on how LRRK2 affects the axonal transport of different cargoes, focusing on synaptic vesicle precursors, mitochondria, and autophagosomes. We further discuss how LRRK2 influences cytoskeletal dynamics and how it affects vesicle trafficking at the Golgi, which may indirectly contribute to its effect on axonal transport. This review summarizes our current understanding of how pathogenic LRRK2 hyperactivation disrupts axonal transport and how this may be linked to the neurodegeneration of PD.<\/jats:p>","DOI":"10.1042\/bcj20253133","type":"journal-article","created":{"date-parts":[[2025,7,2]],"date-time":"2025-07-02T13:48:28Z","timestamp":1751464108000},"page":"905-919","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Role of LRRK2 in axonal transport and Parkinson\u2019s disease"],"prefix":"10.1042","volume":"482","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-5131-8796","authenticated-orcid":false,"given":"Bj\u00f6rn","family":"Twellsieck","sequence":"first","affiliation":[{"name":"1Department of Neurology, University Medical Center Goettingen, 37077 Goettingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9701-5273","authenticated-orcid":false,"given":"C. Alexander","family":"Boecker","sequence":"additional","affiliation":[{"name":"1Department of Neurology, University Medical Center Goettingen, 37077 Goettingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2025,6,25]]},"reference":[{"key":"2025070209263824400_BCJ-2025-3133C1","doi-asserted-by":"crossref","first-page":"5858","DOI":"10.1523\/JNEUROSCI.17-15-05858.1997","article-title":"Quantitative ultrastructural analysis of hippocampal excitatory synapses","volume":"17","author":"Schikorski","year":"1997","journal-title":"J. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C2","article-title":"Complete morphologies of basal forebrain cholinergic neurons in the mouse","volume":"3","author":"Wu","year":"2014","journal-title":"elife, eLife Sciences Publications Ltd"},{"key":"2025070209263824400_BCJ-2025-3133C3","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1038\/nrm2774","article-title":"Kinesin superfamily motor proteins and intracellular transport","volume":"10","author":"Hirokawa","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C4","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1083\/jcb.200408113","article-title":"A standardized kinesin nomenclature","volume":"167","author":"Lawrence","year":"2004","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C5","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1038\/nrm3667","article-title":"Functions and mechanics of dynein motor proteins","volume":"14","author":"Roberts","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C6","doi-asserted-by":"crossref","first-page":"2058","DOI":"10.1093\/brain\/aws133","article-title":"Alterations in axonal transport motor proteins in sporadic and experimental Parkinson\u2019s disease","volume":"135","author":"Chu","year":"2012","journal-title":"Brain (Bacau)"},{"key":"2025070209263824400_BCJ-2025-3133C7","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1097\/00005072-198409000-00001","article-title":"Fine structural observations of neurofilamentous changes in amyotrophic lateral sclerosis","volume":"43","author":"Hirano","year":"1984","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"2025070209263824400_BCJ-2025-3133C8","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1126\/science.1105681","article-title":"Axonopathy and transport deficits early in the pathogenesis of Alzheimer\u2019s disease","volume":"307","author":"Stokin","year":"2005","journal-title":"Science"},{"key":"2025070209263824400_BCJ-2025-3133C9","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0896-6273(03)00569-5","article-title":"Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport","volume":"40","author":"Szebenyi","year":"2003","journal-title":"Neuron"},{"key":"2025070209263824400_BCJ-2025-3133C10","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1038\/ng1341","article-title":"Mutations in the mitochondrial GTPase mitofusin 2 cause charcot-marie-tooth neuropathy type 2A","volume":"36","author":"Z\u00fcchner","year":"2004","journal-title":"Nat. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C11","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/S0140-6736(14)61393-3","article-title":"Parkinson\u2019s disease","volume":"386","author":"Kalia","year":"2015","journal-title":"The Lancet"},{"key":"2025070209263824400_BCJ-2025-3133C12","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/j.tins.2006.03.006","article-title":"LRRK2 in Parkinson\u2019s disease: protein domains and functional insights","volume":"29","author":"Mata","year":"2006","journal-title":"Trends Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C13","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1212\/01.WNL.0000167552.79769.b3","article-title":"LRRK2 gene in Parkinson disease: mutation analysis and case control association study","volume":"65","author":"Pais\u00e1n-Ru\u00edz","year":"2005","journal-title":"Neurology (ECronicon)."},{"key":"2025070209263824400_BCJ-2025-3133C14","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.neuron.2004.11.005","article-title":"Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology","volume":"44","author":"Zimprich","year":"2004","journal-title":"Neuron, Elsevier"},{"key":"2025070209263824400_BCJ-2025-3133C15","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1177\/1073858415616558","article-title":"LRRK2 at the crossroad between autophagy and microtubule trafficking: insights into Parkinson\u2019s disease","volume":"23","author":"Esteves","year":"2017","journal-title":"Neuroscientist"},{"key":"2025070209263824400_BCJ-2025-3133C16","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1042\/BCJ20220161","article-title":"Impact of 100 LRRK2 variants linked to Parkinson\u2019s disease on kinase activity and microtubule binding","volume":"479","author":"Kalogeropulou","year":"2022","journal-title":"Biochem. J."},{"key":"2025070209263824400_BCJ-2025-3133C17","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1093\/hmg\/ddi439","article-title":"The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity","volume":"15","author":"Gloeckner","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C18","doi-asserted-by":"crossref","first-page":"2671","DOI":"10.1042\/BCJ20160557","article-title":"Phos-tag analysis of Rab10 phosphorylation by LRRK2: a powerful assay for assessing kinase function and inhibitors","volume":"473","author":"Ito","year":"2016","journal-title":"Biochem. J."},{"key":"2025070209263824400_BCJ-2025-3133C19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BCJ20170802","article-title":"Development of phospho-specific Rab protein antibodies to monitor in vivo activity of the LRRK2 Parkinson\u2019s disease kinase","volume":"475","author":"Lis","year":"2018","journal-title":"Biochem. J."},{"key":"2025070209263824400_BCJ-2025-3133C20","doi-asserted-by":"crossref","first-page":"16842","DOI":"10.1073\/pnas.0507360102","article-title":"Parkinson\u2019s disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity","volume":"102","author":"West","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2025070209263824400_BCJ-2025-3133C21","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev-biochem-030122-051144","article-title":"Leucine-rich repeat kinases","volume":"93","author":"Alessi","year":"2024","journal-title":"Annu. Rev. Biochem."},{"key":"2025070209263824400_BCJ-2025-3133C22","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.12813","article-title":"Phosphoproteomics reveals that Parkinson\u2019s disease kinase LRRK2 regulates a subset of Rab GTPases","volume":"5","author":"Steger","year":"2016","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C23","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.31012","article-title":"Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis","volume":"6","author":"Steger","year":"2017","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C24","doi-asserted-by":"crossref","DOI":"10.3389\/fneur.2018.00455","article-title":"On cell loss and selective vulnerability of neuronal populations in Parkinson\u2019s disease","volume":"9","author":"Gigu\u00e8re","year":"2018","journal-title":"Front. Neurol."},{"key":"2025070209263824400_BCJ-2025-3133C25","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1523\/JNEUROSCI.4029-08.2009","article-title":"Single nigrostriatal dopaminergic neurons form widely spread and highly dense axonal arborizations in the neostriatum","volume":"29","author":"Matsuda","year":"2009","journal-title":"J. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C26","first-page":"3171","article-title":"Cellular functions of Rab GTPases at a glance","volume":"128","author":"Zhen","year":"2015","journal-title":"J. Cell. Sci."},{"key":"2025070209263824400_BCJ-2025-3133C27","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.ceb.2019.03.004","article-title":"Rab regulation by GEFs and GAPs during membrane traffic","volume":"59","author":"Lamber","year":"2019","journal-title":"Curr. Opin. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C28","doi-asserted-by":"crossref","first-page":"2626","DOI":"10.1073\/pnas.1318306111","article-title":"Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease","volume":"111","author":"Beilina","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2025070209263824400_BCJ-2025-3133C29","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.semcdb.2010.10.003","article-title":"GTPases involved in vesicular trafficking: structures and mechanisms","volume":"22","author":"Itzen","year":"2011","journal-title":"Semin. Cell Dev. Biol."},{"key":"2025070209263824400_BCJ-2025-3133C30","doi-asserted-by":"crossref","DOI":"10.1186\/s13024-018-0235-y","article-title":"Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation","volume":"13","author":"Madero-P\u00e9rez","year":"2018","journal-title":"Mol. Neurodegener."},{"key":"2025070209263824400_BCJ-2025-3133C31","doi-asserted-by":"crossref","first-page":"E9115","DOI":"10.1073\/pnas.1812196115","article-title":"LRRK2 and its substrate Rab GTPases are sequentially targeted onto stressed lysosomes and maintain their homeostasis","volume":"115","author":"Eguchi","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2025070209263824400_BCJ-2025-3133C32","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.str.2020.01.005","article-title":"Structural basis for Rab8a recruitment of RILPL2 via LRRK2 phosphorylation of switch 2","volume":"28","author":"Waschb\u00fcsch","year":"2020","journal-title":"Structure"},{"key":"2025070209263824400_BCJ-2025-3133C33","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-10501-z","article-title":"Selective LRRK2 kinase inhibition reduces phosphorylation of endogenous Rab10 and Rab12 in human peripheral mononuclear blood cells","volume":"7","author":"Thirstrup","year":"2017","journal-title":"Sci. Rep."},{"key":"2025070209263824400_BCJ-2025-3133C34","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1080\/21541248.2019.1666623","article-title":"LRRK2 binds to the Rab32 subfamily in a GTP-dependent manner via its armadillo domain","volume":"12","author":"McGrath","year":"2021","journal-title":"Small GTPases"},{"key":"2025070209263824400_BCJ-2025-3133C35","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.79771","article-title":"A feed-forward pathway drives LRRK2 kinase membrane recruitment and activation","volume":"11","author":"Vides","year":"2022","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C36","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.87098","article-title":"Genome-wide screen reveals Rab12 GTPase as a critical activator of Parkinson\u2019s disease-linked LRRK2 kinase","volume":"12","author":"Dhekne","year":"2023","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C37","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.87255","article-title":"Rab12 is a regulator of LRRK2 and its activation by damaged lysosomes","volume":"12","author":"Wang","year":"2023","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C38","doi-asserted-by":"crossref","first-page":"102482","DOI":"10.1016\/j.ceb.2025.102482","article-title":"LRRK2, lysosome damage, and Parkinson\u2019s disease","volume":"93","author":"Bentley-DeSousa","year":"2025","journal-title":"Curr. Opin. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C39","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1016\/S1474-4422(24)00121-2","article-title":"RAB32 Ser71Arg in autosomal dominant Parkinson\u2019s disease: linkage, association, and functional analyses","volume":"23","author":"Gustavsson","year":"2024","journal-title":"Lancet Neurol."},{"key":"2025070209263824400_BCJ-2025-3133C40","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1038\/s41588-024-01787-7","article-title":"Systematic rare variant analyses identify RAB32 as a susceptibility gene for familial Parkinson\u2019s disease","volume":"56","author":"Hop","year":"2024","journal-title":"Nat. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C41","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1038\/ng.487","article-title":"Genome-wide association study reveals genetic risk underlying Parkinson\u2019s disease","volume":"41","author":"Sim\u00f3n-S\u00e1nchez","year":"2009","journal-title":"Nat. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C42","doi-asserted-by":"crossref","first-page":"1356","DOI":"10.1038\/ejhg.2010.125","article-title":"Genetic variability at the PARK16 locus","volume":"18","author":"Tucci","year":"2010","journal-title":"Eur. J. Hum. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C43","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202310150","article-title":"A STING-CASM-GABARAP pathway activates LRRK2 at lysosomes","volume":"224","author":"Bentley-DeSousa","year":"2025","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C44","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202302067","article-title":"The V-ATPase-ATG16L1 axis recruits LRRK2 to facilitate the lysosomal stress response","volume":"223","author":"Eguchi","year":"2024","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C45","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1093\/hmg\/ddr526","article-title":"LRRK2 Parkinson disease mutations enhance its microtubule association","volume":"21","author":"Kett","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C46","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1016\/j.cell.2020.08.004","article-title":"The in situ structure of Parkinson\u2019s disease-linked LRRK2","volume":"182","author":"Watanabe","year":"2020","journal-title":"Cell"},{"key":"2025070209263824400_BCJ-2025-3133C47","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1038\/s41594-022-00863-y","article-title":"Structural basis for Parkinson\u2019s disease-linked LRRK2\u2019s binding to microtubules","volume":"29","author":"Snead","year":"2022","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2025070209263824400_BCJ-2025-3133C48","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1038\/s41586-020-2673-2","article-title":"Structure of LRRK2 in Parkinson\u2019s disease and model for microtubule interaction","volume":"588","author":"Deniston","year":"2020","journal-title":"Nature"},{"key":"2025070209263824400_BCJ-2025-3133C49","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1124\/jpet.115.227587","article-title":"MLi-2, a potent, selective, and centrally active compound for exploring the therapeutic potential and safety of LRRK2 kinase inhibition","volume":"355","author":"Fell","year":"2015","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"2025070209263824400_BCJ-2025-3133C50","doi-asserted-by":"crossref","first-page":"14979","DOI":"10.1073\/pnas.1900289116","article-title":"The dynamic switch mechanism that leads to activation of LRRK2 is embedded in the DFG\u03c8 motif in the kinase domain","volume":"116","author":"Schmidt","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2025070209263824400_BCJ-2025-3133C51","doi-asserted-by":"crossref","first-page":"2983","DOI":"10.1021\/acs.jmedchem.7b00045","article-title":"Discovery of a 3-(4-Pyrimidinyl) indazole (MLi-2), an Orally Available and Selective Leucine-Rich Repeat Kinase 2 (LRRK2) inhibitor that reduces brain kinase activity","volume":"60","author":"Scott","year":"2017","journal-title":"J. Med. Chem."},{"key":"2025070209263824400_BCJ-2025-3133C52","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1016\/j.cub.2021.02.061","article-title":"Increased LRRK2 kinase activity alters neuronal autophagy by disrupting the axonal transport of autophagosomes","volume":"31","author":"Boecker","year":"2021","journal-title":"Curr. Biol."},{"key":"2025070209263824400_BCJ-2025-3133C53","doi-asserted-by":"crossref","first-page":"112448","DOI":"10.1016\/j.celrep.2023.112448","article-title":"Regulatory imbalance between LRRK2 kinase, PPM1H phosphatase, and ARF6 GTPase disrupts the axonal transport of autophagosomes","volume":"42","author":"Dou","year":"2023","journal-title":"Cell Rep."},{"key":"2025070209263824400_BCJ-2025-3133C54","doi-asserted-by":"crossref","unstructured":"Fricke, M., Mechel, A., Twellsieck, B., Grein, J.M., Cima-Omori, M.S., Zweckstetter, M.et al. (2024) Knockout of the LRRK2-counteracting RAB phosphatase PPM1H disrupts axonal autophagy and exacerbates alpha-synuclein aggregation. bioRxiv. https:\/\/doi.org\/10.1101\/2024.10.14.618089","DOI":"10.1101\/2024.10.14.618089"},{"key":"2025070209263824400_BCJ-2025-3133C55","doi-asserted-by":"crossref","first-page":"4157","DOI":"10.1083\/jcb.201902184","article-title":"Membrane association but not identity is required for LRRK2 activation and phosphorylation of Rab GTPases","volume":"218","author":"Gomez","year":"2019","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C56","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1093\/hmg\/ddx410","article-title":"LRRK2 phosphorylates membrane-bound Rabs and is activated by GTP-bound Rab7L1 to promote recruitment to the trans-Golgi network","volume":"27","author":"Liu","year":"2018","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C57","doi-asserted-by":"crossref","first-page":"1","DOI":"10.15252\/embj.201798099","article-title":"Rab29 activation of the Parkinson\u2019s disease-associated LRRK2 kinase","volume":"37","author":"Purlyte","year":"2018","journal-title":"EMBO J."},{"key":"2025070209263824400_BCJ-2025-3133C58","doi-asserted-by":"crossref","first-page":"107614","DOI":"10.1016\/j.celrep.2020.107614","article-title":"The Parkinson\u2019s disease protein LRRK2 interacts with the GARP complex to promote retrograde transport to the trans-golgi network","volume":"31","author":"Beilina","year":"2020","journal-title":"Cell Rep."},{"key":"2025070209263824400_BCJ-2025-3133C59","doi-asserted-by":"crossref","first-page":"2063","DOI":"10.1042\/BST20201146","article-title":"LRRK2 along the golgi and lysosome connection: a jamming situation","volume":"49","author":"Piccoli","year":"2021","journal-title":"Biochem. Soc. Trans."},{"key":"2025070209263824400_BCJ-2025-3133C60","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1093\/brain\/awx344","article-title":"Reduced LRRK2 in association with retromer dysfunction in post-mortem brain tissue from LRRK2 mutation carriers","volume":"141","author":"Zhao","year":"2018","journal-title":"Brain (Bacau)"},{"key":"2025070209263824400_BCJ-2025-3133C61","doi-asserted-by":"crossref","first-page":"4397","DOI":"10.1042\/BCJ20200458","article-title":"Endogenous Rab29 does not impact basal or stimulated LRRK2 pathway activity","volume":"477","author":"Kalogeropulou","year":"2020","journal-title":"Biochem. J."},{"key":"2025070209263824400_BCJ-2025-3133C62","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1042\/BCJ20180248","article-title":"The Parkinson\u2019s disease VPS35[D620N] mutation enhances LRRK2-mediated Rab protein phosphorylation in mouse and human","volume":"475","author":"Mir","year":"2018","journal-title":"Biochem. J."},{"key":"2025070209263824400_BCJ-2025-3133C63","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1186\/s13041-021-00848-w","article-title":"Endosomal traffic and glutamate synapse activity are increased in VPS35 D620N mutant knock-in mouse neurons, and resistant to LRRK2 kinase inhibition","volume":"14","author":"Kadgien","year":"2021","journal-title":"Mol. Brain"},{"key":"2025070209263824400_BCJ-2025-3133C64","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1042\/BCJ20230492","article-title":"The Parkinson\u2019s disease related mutant VPS35 (D620N) amplifies the LRRK2 response to endolysosomal stress","volume":"481","author":"McCarron","year":"2024","journal-title":"Biochem. J."},{"key":"2025070209263824400_BCJ-2025-3133C65","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41531-023-00609-7","article-title":"Inhibition of LRRK2 kinase activity rescues deficits in striatal dopamine physiology in VPS35 p.D620N knock-in mice","volume":"9","author":"Bu","year":"2023","journal-title":"NPJ Parkinsons. Dis."},{"key":"2025070209263824400_BCJ-2025-3133C66","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adj1205","article-title":"Parkinson\u2019s VPS35[D620N] mutation induces LRRK2-mediated lysosomal association of RILPL1 and TMEM55B","volume":"9","author":"Pal","year":"2023","journal-title":"Sci. Adv."},{"key":"2025070209263824400_BCJ-2025-3133C67","doi-asserted-by":"crossref","DOI":"10.15252\/embj.201798044","article-title":"Newly produced synaptic vesicle proteins are preferentially used in synaptic transmission","volume":"37","author":"Truckenbrodt","year":"2018","journal-title":"EMBO J."},{"key":"2025070209263824400_BCJ-2025-3133C68","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1083\/jcb.140.3.659","article-title":"Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons","volume":"140","author":"Nakata","year":"1998","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C69","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1038\/ncb1785","article-title":"KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN\/MADD","volume":"10","author":"Niwa","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C70","doi-asserted-by":"crossref","DOI":"10.1126\/science.aaw9997","article-title":"Axonal transport: driving synaptic function","volume":"366","author":"Guedes-Dias","year":"2019","journal-title":"Science"},{"key":"2025070209263824400_BCJ-2025-3133C71","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1523\/JNEUROSCI.3553-05.2006","article-title":"Rab3 superprimes synaptic vesicles for release: implications for short-term synaptic plasticity","volume":"26","author":"Schl\u00fcter","year":"2006","journal-title":"J. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C72","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202105011","article-title":"Specific KIF1A-adaptor interactions control selective cargo recognition","volume":"220","author":"Hummel","year":"2021","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C73","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202307092","article-title":"RAB3 phosphorylation by pathogenic LRRK2 impairs trafficking of synaptic vesicle precursors","volume":"223","author":"Dou","year":"2024","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C74","doi-asserted-by":"crossref","DOI":"10.1186\/s40478-021-01283-7","article-title":"Inhibition of LRRK2 kinase activity promotes anterograde axonal transport and presynaptic targeting of \u03b1-synuclein","volume":"9","author":"Brzozowski","year":"2021","journal-title":"Acta Neuropathol. Commun."},{"key":"2025070209263824400_BCJ-2025-3133C75","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1111\/jnc.15240","article-title":"LRRK2 at the pre-synaptic site: a 16-years perspective","volume":"157","author":"Pischedda","year":"2021","journal-title":"J. Neurochem."},{"key":"2025070209263824400_BCJ-2025-3133C76","first-page":"541","article-title":"LRRK2 functions in synaptic vesicle endocytosis through a kinase-dependent mechanism","volume":"128","author":"Arranz","year":"2015","journal-title":"J. Cell. Sci."},{"key":"2025070209263824400_BCJ-2025-3133C77","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fncel.2014.00301","article-title":"Synaptic function is modulated by LRRK2 and glutamate release is increased in cortical neurons of G2019S LRRK2 knock-in mice","volume":"8","author":"Beccano-Kelly","year":"2014","journal-title":"Front. Cell. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C78","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fnmol.2016.00035","article-title":"LRRK2 regulates voltage-gated calcium channel function","volume":"9","author":"Bedford","year":"2016","journal-title":"Front. Mol. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C79","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13024-015-0066-z","article-title":"LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate","volume":"11","author":"Belluzzi","year":"2016","journal-title":"Mol. Neurodegener."},{"key":"2025070209263824400_BCJ-2025-3133C80","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2020.104948","article-title":"Sequential screening nominates the Parkinson\u2019s disease associated kinase LRRK2 as a regulator of Clathrin-mediated endocytosis","volume":"141","author":"Heaton","year":"2020","journal-title":"Neurobiol. Dis."},{"key":"2025070209263824400_BCJ-2025-3133C81","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1111\/jnc.14778","article-title":"Leucine-rich repeat kinase 2 phosphorylation on synapsin I regulates glutamate release at pre-synaptic sites","volume":"150","author":"Marte","year":"2019","journal-title":"J. Neurochem."},{"key":"2025070209263824400_BCJ-2025-3133C82","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1016\/j.neuron.2012.08.022","article-title":"LRRK2 controls an EndoA phosphorylation cycle in synaptic endocytosis","volume":"75","author":"Matta","year":"2012","journal-title":"Neuron"},{"key":"2025070209263824400_BCJ-2025-3133C83","doi-asserted-by":"crossref","first-page":"5576","DOI":"10.1073\/pnas.1717590115","article-title":"LRRK2 phosphorylation of auxilin mediates synaptic defects in dopaminergic neurons from patients with Parkinson\u2019s disease","volume":"115","author":"Nguyen","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2025070209263824400_BCJ-2025-3133C84","doi-asserted-by":"crossref","first-page":"1988","DOI":"10.1073\/pnas.87.5.1988","article-title":"rab3 is a small GTP-binding protein exclusively localized to synaptic vesicles","volume":"87","author":"Fischer von Mollard","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2025070209263824400_BCJ-2025-3133C85","doi-asserted-by":"crossref","first-page":"1356","DOI":"10.1111\/j.1600-0854.2011.01237.x","article-title":"Involvement of Rab3A in vesicle priming during exocytosis: interaction with Munc13-1 and Munc18-1","volume":"12","author":"Huang","year":"2011","journal-title":"Traffic"},{"key":"2025070209263824400_BCJ-2025-3133C86","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1016\/j.neuron.2019.09.015","article-title":"The RAB3-RIM pathway is essential for the release of neuromodulators","volume":"104","author":"Persoon","year":"2019","journal-title":"Neuron"},{"key":"2025070209263824400_BCJ-2025-3133C87","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0000616","article-title":"The role of Rab3a in secretory vesicle docking requires association\/dissociation of guanidine phosphates and Munc18-1","volume":"2","author":"van Weering","year":"2007","journal-title":"Plos One"},{"key":"2025070209263824400_BCJ-2025-3133C88","doi-asserted-by":"crossref","first-page":"19055","DOI":"10.1073\/pnas.1007037107","article-title":"Endosomal sorting of readily releasable synaptic vesicles","volume":"107","author":"Hoopmann","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2025070209263824400_BCJ-2025-3133C89","doi-asserted-by":"crossref","first-page":"3583","DOI":"10.1242\/jcs.00676","article-title":"An essential role of Rab5 in uniformity of synaptic vesicle size","volume":"116","author":"Shimizu","year":"2003","journal-title":"J. Cell. Sci."},{"key":"2025070209263824400_BCJ-2025-3133C90","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1083\/jcb.200211087","article-title":"Role of drosophila Rab5 during endosomal trafficking at the synapse and evoked neurotransmitter release","volume":"161","author":"Wucherpfennig","year":"2003","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C91","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.94930.3","article-title":"Rab10 regulates neuropeptide release by maintaining Ca2+ homeostasis and protein synthesis","volume":"13","author":"Dong","year":"2025","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C92","doi-asserted-by":"crossref","DOI":"10.1186\/s40478-023-01704-9","article-title":"Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain","volume":"11","author":"Singh","year":"2023","journal-title":"Acta Neuropathol. Commun."},{"key":"2025070209263824400_BCJ-2025-3133C93","doi-asserted-by":"crossref","first-page":"8668","DOI":"10.1523\/JNEUROSCI.0725-16.2016","article-title":"Activity-dependent degradation of synaptic vesicle proteins requires Rab35 and the ESCRT pathway","volume":"36","author":"Sheehan","year":"2016","journal-title":"J. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C94","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.cell.2011.02.039","article-title":"Loss of skywalker reveals synaptic endosomes as sorting stations for synaptic vesicle proteins","volume":"145","author":"Uytterhoeven","year":"2011","journal-title":"Cell"},{"key":"2025070209263824400_BCJ-2025-3133C95","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.neuron.2021.12.029","article-title":"Brain-derived autophagosome profiling reveals the engulfment of nucleoid-enriched mitochondrial fragments by basal autophagy in neurons","volume":"110","author":"Goldsmith","year":"2022","journal-title":"Neuron"},{"key":"2025070209263824400_BCJ-2025-3133C96","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.22234","article-title":"Regulation of mitochondria-dynactin interaction and mitochondrial retrograde transport in axons","volume":"6","author":"Drerup","year":"2017","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C97","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1007\/s10048-012-0324-y","article-title":"Axonal transport deficit in a KIF5A( -\/- ) mouse model","volume":"13","author":"Karle","year":"2012","journal-title":"Neurogenetics"},{"key":"2025070209263824400_BCJ-2025-3133C98","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1016\/S0092-8674(00)81459-2","article-title":"Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria","volume":"93","author":"Tanaka","year":"1998","journal-title":"Cell"},{"key":"2025070209263824400_BCJ-2025-3133C99","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1083\/jcb.201302040","article-title":"Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport","volume":"202","author":"Chen","year":"2013","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C100","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.neuron.2012.11.027","article-title":"TRAK\/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites","volume":"77","author":"Mikhaylova","year":"2013","journal-title":"Neuron"},{"key":"2025070209263824400_BCJ-2025-3133C101","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/0306-4522(91)90143-C","article-title":"Cytoplasmic architecture of the axon terminal: filamentous strands specifically associated with synaptic vesicles","volume":"40","author":"Gotow","year":"1991","journal-title":"Neuroscience"},{"key":"2025070209263824400_BCJ-2025-3133C102","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1242\/jcs.104.3.917","article-title":"The regulation of bidirectional mitochondrial transport is coordinated with axonal outgrowth","volume":"104","author":"Morris","year":"1993","journal-title":"J. Cell. Sci."},{"key":"2025070209263824400_BCJ-2025-3133C103","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2018100875","article-title":"LRRK2 regulates endoplasmic reticulum-mitochondrial tethering through the PERK-mediated ubiquitination pathway","volume":"39","author":"Toyofuku","year":"2020","journal-title":"EMBO J."},{"key":"2025070209263824400_BCJ-2025-3133C104","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1038\/s41401-024-01359-9","article-title":"The correlation between mitochondria-associated endoplasmic reticulum membranes (MAMs) and Ca2+ transport in the pathogenesis of diseases","volume":"46","author":"Zhao","year":"2025","journal-title":"Acta Pharmacol. Sin."},{"key":"2025070209263824400_BCJ-2025-3133C105","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms6245","article-title":"Increasing microtubule acetylation rescues axonal transport and locomotor deficits caused by LRRK2 Roc-COR domain mutations","volume":"5","author":"Godena","year":"2014","journal-title":"Nat. Commun."},{"key":"2025070209263824400_BCJ-2025-3133C106","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/j.stem.2016.08.002","article-title":"Functional impairment in miro degradation and mitophagy is a shared feature in familial and sporadic parkinson\u2019s disease","volume":"19","author":"Hsieh","year":"2016","journal-title":"Cell Stem Cell"},{"key":"2025070209263824400_BCJ-2025-3133C107","doi-asserted-by":"crossref","first-page":"2808","DOI":"10.1093\/hmg\/ddad102","article-title":"Mitochondrial dysfunction and mitophagy defects in LRRK2-R1441C Parkinson\u2019s disease models","volume":"32","author":"Williamson","year":"2023","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C108","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1083\/jcb.201106120","article-title":"Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons","volume":"196","author":"Maday","year":"2012","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C109","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.devcel.2014.06.001","article-title":"Autophagosome biogenesis in primary neurons follows an ordered and spatially regulated pathway","volume":"30","author":"Maday","year":"2014","journal-title":"Dev. Cell"},{"key":"2025070209263824400_BCJ-2025-3133C110","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1083\/jcb.201606082","article-title":"A STRIPAK complex mediates axonal transport of autophagosomes and dense core vesicles through PP2A regulation","volume":"216","author":"Neisch","year":"2017","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C111","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.devcel.2016.06.012","article-title":"KIF1A\/UNC-104 transports ATG-9 to regulate neurodevelopment and autophagy at synapses","volume":"38","author":"Stavoe","year":"2016","journal-title":"Dev. Cell"},{"key":"2025070209263824400_BCJ-2025-3133C112","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1080\/15548627.2019.1703354","article-title":"Differential regulation of autophagy during metabolic stress in astrocytes and neurons","volume":"16","author":"Kulkarni","year":"2020","journal-title":"Autophagy"},{"key":"2025070209263824400_BCJ-2025-3133C113","doi-asserted-by":"crossref","first-page":"5933","DOI":"10.1523\/JNEUROSCI.4401-15.2016","article-title":"Compartment-specific regulation of autophagy in porimary neurons","volume":"36","author":"Maday","year":"2016","journal-title":"J. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C114","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202010179","article-title":"Sequential dynein effectors regulate axonal autophagosome motility in a maturation-dependent pathway","volume":"220","author":"Cason","year":"2021","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C115","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202301084","article-title":"Axonal transport of autophagosomes is regulated by dynein activators JIP3\/JIP4 and ARF\/RAB GTPases","volume":"222","author":"Cason","year":"2023","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C116","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.neuron.2012.02.025","article-title":"Dynactin is required for transport initiation from the distal axon","volume":"74","author":"Moughamian","year":"2012","journal-title":"Neuron"},{"key":"2025070209263824400_BCJ-2025-3133C117","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/j.cub.2010.02.058","article-title":"Motor coordination via a tug-of-war mechanism drives bidirectional vesicle transport","volume":"20","author":"Hendricks","year":"2010","journal-title":"Curr. Biol."},{"key":"2025070209263824400_BCJ-2025-3133C118","doi-asserted-by":"crossref","DOI":"10.1091\/mbc.E22-03-0111","article-title":"Spatiotemporal analysis of axonal autophagosome-lysosome dynamics reveals limited fusion events and slow maturation","volume":"33","author":"Cason","year":"2022","journal-title":"Mol. Biol. Cell"},{"key":"2025070209263824400_BCJ-2025-3133C119","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.celrep.2019.06.013","article-title":"Neuronal soma-derived degradative lysosomes are continuously delivered to distal axons to maintain local degradation capacity","volume":"28","author":"Farfel-Becker","year":"2019","journal-title":"Cell Rep."},{"key":"2025070209263824400_BCJ-2025-3133C120","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1016\/j.devcel.2014.04.015","article-title":"LC3 binding to the scaffolding protein JIP1 regulates processive dynein-driven transport of autophagosomes","volume":"29","author":"Fu","year":"2014","journal-title":"Dev. Cell"},{"key":"2025070209263824400_BCJ-2025-3133C121","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1523\/JNEUROSCI.1870-13.2014","article-title":"The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation","volume":"34","author":"Wong","year":"2014","journal-title":"J. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C122","doi-asserted-by":"crossref","first-page":"4022","DOI":"10.1093\/hmg\/ddp346","article-title":"LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model","volume":"18","author":"Alegre-Abarrategui","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C123","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1111\/j.1471-4159.2008.05217.x","article-title":"Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells","volume":"105","author":"Plowey","year":"2008","journal-title":"J. Neurochem."},{"key":"2025070209263824400_BCJ-2025-3133C124","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0018568","article-title":"Dopaminergic neuronal loss, reduced neurite complexity and autophagic abnormalities in transgenic mice expressing G2019S mutant LRRK2","volume":"6","author":"Ramonet","year":"2011","journal-title":"Plos One"},{"key":"2025070209263824400_BCJ-2025-3133C125","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/s00018-012-1061-y","article-title":"The LRRK2 G2019S mutant exacerbates basal autophagy through activation of the MEK\/ERK pathway","volume":"70","author":"Bravo-San Pedro","year":"2013","journal-title":"Cell. Mol. Life Sci."},{"key":"2025070209263824400_BCJ-2025-3133C126","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1093\/hmg\/ddr481","article-title":"Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP","volume":"21","author":"G\u00f3mez-Suaga","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C127","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2020.00498","article-title":"LRRK2: autophagy and lysosomal activity","volume":"14","author":"Madureira","year":"2020","journal-title":"Front. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C128","doi-asserted-by":"crossref","first-page":"2900","DOI":"10.1016\/j.bbamcr.2013.07.020","article-title":"Inhibition of LRRK2 kinase activity stimulates macroautophagy","volume":"1833","author":"Manzoni","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"2025070209263824400_BCJ-2025-3133C129","doi-asserted-by":"crossref","DOI":"10.1038\/srep35106","article-title":"mTOR independent regulation of macroautophagy by leucine rich Repeat kinase 2 via beclin-1","volume":"6","author":"Manzoni","year":"2016","journal-title":"Sci. Rep."},{"key":"2025070209263824400_BCJ-2025-3133C130","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1038\/nn.3350","article-title":"Interplay of LRRK2 with chaperone-mediated autophagy","volume":"16","author":"Orenstein","year":"2013","journal-title":"Nat. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C131","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.bbadis.2014.11.009","article-title":"Threonine 56 phosphorylation of Bcl-2 is required for LRRK2 G2019S-induced mitochondrial depolarization and autophagy","volume":"1852","author":"Su","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"2025070209263824400_BCJ-2025-3133C132","doi-asserted-by":"crossref","first-page":"4545","DOI":"10.1093\/hmg\/ddt301","article-title":"Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation","volume":"22","author":"Su","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C133","doi-asserted-by":"crossref","first-page":"2696","DOI":"10.1093\/hmg\/ddz088","article-title":"LRRK2 interacts with the vacuolar-type H+-ATPase pump a1 subunit to regulate lysosomal function","volume":"28","author":"Wallings","year":"2019","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C134","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.tox.2014.07.001","article-title":"G2019S LRRK2 mutant fibroblasts from Parkinson\u2019s disease patients show increased sensitivity to neurotoxin 1-methyl-4-phenylpyridinium dependent of autophagy","volume":"324","author":"Yakhine-Diop","year":"2014","journal-title":"Toxicology"},{"key":"2025070209263824400_BCJ-2025-3133C135","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1126\/sciadv.abb2454","article-title":"LRRK2 mediates tubulation and vesicle sorting from lysosomes","volume":"6","author":"Bonet-Ponce","year":"2020","journal-title":"Sci. Adv."},{"key":"2025070209263824400_BCJ-2025-3133C136","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.cub.2008.12.043","article-title":"ARF6 Interacts with JIP4 to control a motor switch mechanism regulating endosome traffic in cytokinesis","volume":"19","author":"Montagnac","year":"2009","journal-title":"Curr. Biol."},{"key":"2025070209263824400_BCJ-2025-3133C137","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1111\/tra.12701","article-title":"ToolBox: Live Imaging of intracellular organelle transport in induced pluripotent stem cell-derived neurons","volume":"21","author":"Boecker","year":"2020","journal-title":"Traffic"},{"key":"2025070209263824400_BCJ-2025-3133C138","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1083\/jcb.202010179","article-title":"Sequential dynein effectors regulate axonal autophagosome motility in a maturation-dependent pathway","volume":"220","author":"Cason","year":"2021","journal-title":"J. Cell Biol."},{"key":"2025070209263824400_BCJ-2025-3133C139","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.44219","article-title":"Expression of WIPI2B counteracts age-related decline in autophagosome biogenesis in neurons","volume":"8","author":"Stavoe","year":"2019","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C140","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/15548627.2023.2236485","article-title":"Aging differentially affects axonal autophagosome formation and maturation","volume":"19","author":"Tsong","year":"2023","journal-title":"Autophagy"},{"key":"2025070209263824400_BCJ-2025-3133C141","doi-asserted-by":"crossref","unstructured":"Palumbos, S.D., Popolow, J., Goldsmith, J. and Holzbaur, E.L.F. (2024) Autophagic stress activates distinct compensatory secretory pathways in neurons. 2024.11.07.621551bioRxiv. https:\/\/doi.org\/10.1101\/2024.11.07.621551","DOI":"10.1101\/2024.11.07.621551"},{"key":"2025070209263824400_BCJ-2025-3133C142","doi-asserted-by":"crossref","first-page":"7585","DOI":"10.1523\/JNEUROSCI.5809-11.2012","article-title":"Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of \u03b1-synuclein and LRRK2 in the brain","volume":"32","author":"Friedman","year":"2012","journal-title":"J. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C143","doi-asserted-by":"crossref","unstructured":"Goldsmith, J., Ordureau, A., Boecker,, C.A., Arany, M., Harper, J.W. and Holzbaur, E.L. (2022) Proteomics analysis of autophagy cargos reveals distinct adaptations in PINK1 and LRRK2 models of Parkinson disease. 2022\u201310bioRxiv. https:\/\/doi.org\/10.1101\/2022.10.03.510717","DOI":"10.1101\/2022.10.03.510717"},{"key":"2025070209263824400_BCJ-2025-3133C144","doi-asserted-by":"crossref","first-page":"23542","DOI":"10.1074\/jbc.M801992200","article-title":"Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells","volume":"283","author":"Vogiatzi","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2025070209263824400_BCJ-2025-3133C145","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.nbd.2017.12.005","article-title":"Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble \u03b1-synuclein in neurons","volume":"111","author":"Schapansky","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"2025070209263824400_BCJ-2025-3133C146","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1007\/s00401-019-01995-0","article-title":"LRRK2 modifies \u03b1-syn pathology and spread in mouse models and human neurons","volume":"137","author":"Bieri","year":"2019","journal-title":"Acta Neuropathol."},{"key":"2025070209263824400_BCJ-2025-3133C147","doi-asserted-by":"crossref","DOI":"10.1186\/s40478-018-0550-0","article-title":"LRRK2 activity does not dramatically alter \u03b1-synuclein pathology in primary neurons","volume":"6","author":"Henderson","year":"2018","journal-title":"Acta Neuropathol. Commun."},{"key":"2025070209263824400_BCJ-2025-3133C148","doi-asserted-by":"crossref","DOI":"10.1093\/braincomms\/fcz052","article-title":"Neuron-autonomous susceptibility to induced synuclein aggregation is exacerbated by endogenous Lrrk2 mutations and ameliorated by Lrrk2 genetic knock-out","volume":"2","author":"MacIsaac","year":"2020","journal-title":"Brain Commun."},{"key":"2025070209263824400_BCJ-2025-3133C149","doi-asserted-by":"crossref","first-page":"7415","DOI":"10.1523\/JNEUROSCI.3642-15.2016","article-title":"G2019S-LRRK2 expression augments \u03b1-synuclein sequestration into inclusions in neurons","volume":"36","author":"Volpicelli-Daley","year":"2016","journal-title":"J. Neurosci."},{"key":"2025070209263824400_BCJ-2025-3133C150","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1007\/s00401-020-02227-6","article-title":"Neuronal activity modulates alpha-synuclein aggregation and spreading in organotypic brain slice cultures and in vivo","volume":"140","author":"Wu","year":"2020","journal-title":"Acta Neuropathol."},{"key":"2025070209263824400_BCJ-2025-3133C151","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1126\/sciadv.abg6677","article-title":"Computational modeling of tau pathology spread reveals patterns of regional vulnerability and the impact of a genetic risk factor","volume":"7","author":"Cornblath","year":"2021","journal-title":"Sci. Adv."},{"key":"2025070209263824400_BCJ-2025-3133C152","doi-asserted-by":"crossref","DOI":"10.1186\/s40035-024-00403-2","article-title":"LRRK2 kinase inhibition reverses G2019S mutation-dependent effects on tau pathology progression","volume":"13","author":"Lubben","year":"2024","journal-title":"Transl. Neurodegener."},{"key":"2025070209263824400_BCJ-2025-3133C153","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40478-019-0836-x","article-title":"Alzheimer\u2019s disease tau is a prominent pathology in LRRK2 Parkinson\u2019s disease","volume":"7","author":"Henderson","year":"2019","journal-title":"Acta Neuropathol. Commun."},{"key":"2025070209263824400_BCJ-2025-3133C154","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1093\/brain\/awt192","article-title":"Disease duration and the integrity of the nigrostriatal system in Parkinson\u2019s disease","volume":"136","author":"Kordower","year":"2013","journal-title":"Brain (Bacau)"},{"key":"2025070209263824400_BCJ-2025-3133C155","doi-asserted-by":"crossref","first-page":"703","DOI":"10.3233\/JPD-160881","article-title":"Is axonal degeneration a key early event in Parkinson\u2019s disease?","volume":"6","author":"Kurowska","year":"2016","journal-title":"J. Parkinsons. Dis."},{"key":"2025070209263824400_BCJ-2025-3133C156","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1002\/mds.27383","article-title":"Disease modification for Parkinson\u2019s disease: axonal regeneration and trophic factors","volume":"33","author":"Kordower","year":"2018","journal-title":"Mov. Disord."},{"key":"2025070209263824400_BCJ-2025-3133C157","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1002\/mds.27823","article-title":"Neuronal vulnerability in Parkinson disease: Should the focus be on axons and synaptic terminals?","volume":"34","author":"Wong","year":"2019","journal-title":"Mov. Disord."},{"key":"2025070209263824400_BCJ-2025-3133C158","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3233\/JPD-150769","article-title":"Retrograde axonal degeneration in Parkinson disease","volume":"6","author":"Tagliaferro","year":"2016","journal-title":"J. Parkinsons. Dis."},{"key":"2025070209263824400_BCJ-2025-3133C159","doi-asserted-by":"crossref","DOI":"10.3390\/biom13010178","article-title":"Is glial dysfunction the key pathogenesis of LRRK2-linked Parkinson\u2019s disease?","volume":"13","author":"Iseki","year":"2023","journal-title":"Biomolecules"},{"key":"2025070209263824400_BCJ-2025-3133C160","doi-asserted-by":"crossref","unstructured":"Bonet-Ponce, L., Tegicho, T., Beilina, A., Kluss, J.H., Li, Y. and Cookson, M.R. (2024) Opposing actions of JIP4 and RILPL1 provide antagonistic motor force to dynamically regulate membrane reformation during lysosomal tubulation\/sorting driven by LRRK2. https:\/\/doi.org\/10.1101\/2024.04.02.587808","DOI":"10.1101\/2024.04.02.587808"},{"key":"2025070209263824400_BCJ-2025-3133C161","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.67604","article-title":"Pharmacological rescue of impaired mitophagy in Parkinson\u2019s disease-related LRRK2 G2019S knock-in mice","volume":"10","author":"Singh","year":"2021","journal-title":"Elife"},{"key":"2025070209263824400_BCJ-2025-3133C162","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2022.104476","article-title":"Pathogenic LRRK2 regulates centrosome cohesion via Rab10\/RILPL1-mediated CDK5RAP2 displacement","volume":"25","author":"Fdez","year":"2022","journal-title":"iScience"},{"key":"2025070209263824400_BCJ-2025-3133C163","doi-asserted-by":"crossref","first-page":"3552","DOI":"10.1093\/hmg\/ddz201","article-title":"RAB8, RAB10 and RILPL1 contribute to both LRRK2 kinase-mediated centrosomal cohesion and ciliogenesis deficits","volume":"28","author":"Lara Ord\u00f3nez","year":"2019","journal-title":"Hum. Mol. Genet."},{"key":"2025070209263824400_BCJ-2025-3133C164","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2402206121","article-title":"January 16) Loss of primary cilia and dopaminergic neuroprotection in pathogenic LRRK2-driven and idiopathic Parkinson\u2019s disease","volume":"121","author":"Khan","year":"2024","journal-title":"Proc Natl Acad Sci USA"}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/482\/13\/905\/974969\/bcj-2025-3133.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/482\/13\/905\/974969\/bcj-2025-3133.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,7,2]],"date-time":"2025-07-02T13:49:00Z","timestamp":1751464140000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/482\/13\/905\/236246\/Role-of-LRRK2-in-axonal-transport-and-Parkinson-s"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,6,25]]},"references-count":164,"journal-issue":{"issue":"13","published-print":{"date-parts":[[2025,7,2]]}},"URL":"https:\/\/doi.org\/10.1042\/bcj20253133","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2025,7]]},"published":{"date-parts":[[2025,6,25]]}}}