Cited by 269Parkinson's Disease Mechanisms and TreatmentsAutophagy in Disease and TherapyCellular transport and secretion

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VPS35 in Dopamine Neurons Is Required for Endosome-to-Golgi Retrieval of Lamp2a, a Receptor of Chaperone-Mediated Autophagy That Is Critical for -Synuclein Degradation and Prevention of Pathogenesis of Parkinson's Disease

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Tang, F.-L., Erion, J. R., Tian, Y., Liu, W., Yin, D.-M., Ye, J., Tang, B., Mei, L., Xiong, W.-C.·2015·Journal of Neuroscience

DOI 10.1523/jneurosci.0042-15.2015PMC PMC4510296

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Abstract

Vacuolar protein sorting-35 (VPS35) is essential for endosome-to-Golgi retrieval of membrane proteins. Mutations in the VPS35 gene have been identified in patients with autosomal dominant PD. However, it remains poorly understood if and how VPS35 deficiency or mutation contributes to PD pathogenesis. Here we provide evidence that links VPS35 deficiency to PD-like neuropathology. VPS35 was expressed in mouse dopamine (DA) neurons in substantia nigra pars compacta (SNpc) and STR (striatum)--regions that are PD vulnerable. VPS35-deficient mice exhibited PD-relevant deficits including accumulation of α-synuclein in SNpc-DA neurons, loss of DA transmitter and DA neurons in SNpc and STR, and impairment of locomotor behavior. Further mechanical studies showed that VPS35-deficient DA neurons or DA neurons expressing PD-linked VPS35 mutant (D620N) had impaired endosome-to-Golgi retrieval of lysosome-associated membrane glycoprotein 2a (Lamp2a) and accelerated Lamp2a degradation. Expression of Lamp2a in VPS35-deficient DA neurons reduced α-synuclein, supporting the view for Lamp2a as a receptor of chaperone-mediated autophagy to be critical for α-synuclein degradation. These results suggest that VPS35 deficiency or mutation promotes PD pathogenesis and reveals a crucial pathway, VPS35-Lamp2a-α-synuclein, to prevent PD pathogenesis. Significance statement: VPS35 is a key component of the retromer complex that is essential for endosome-to-Golgi retrieval of membrane proteins. Mutations i…

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Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
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Result
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Background
A Mutation in VPS35, Encoding a Subunit of the Retromer Complex, Causes Late-Onset Parkinson Disease
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Additional file 2 of Endosomal traffic and glutamate synapse activity are increased in VPS35 D620N mutant knock-in mouse neurons, and resistant to LRRK2 kinase inhibition
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Additional file 3 of Endosomal dysfunction in iPSC-derived neural cells from Parkinson’s disease patients with VPS35 D620N
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Additional file 4 of VPS35 and α-Synuclein fail to interact to modulate neurodegeneration in rodent models of Parkinson’s disease
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Additional file 15 of Endosomal dysfunction in iPSC-derived neural cells from Parkinson’s disease patients with VPS35 D620N
Bono, K., Hara‐Miyauchi, C., Sumi, S., Oka, H., Iguchi, Y., & Okano, H. (2020) · Figshare · doi:10.6084/m9.figshare.13070791
Additional file 1 of Endosomal dysfunction in iPSC-derived neural cells from Parkinson’s disease patients with VPS35 D620N
Bono, K., Hara‐Miyauchi, C., Sumi, S., Oka, H., Iguchi, Y., & Okano, H. J. (2020) · Figshare · doi:10.6084/m9.figshare.13071229
Additional file 11 of Endosomal dysfunction in iPSC-derived neural cells from Parkinson’s disease patients with VPS35 D620N
Bono, K., Hara‐Miyauchi, C., Sumi, S., Oka, H., Iguchi, Y., & Okano, H. J. (2020) · Figshare · doi:10.6084/m9.figshare.13070785
Additional file 1 of Altered striatal dopamine levels in Parkinson’s disease VPS35 D620N mutant transgenic aged mice
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Additional file 1 of Endosomal traffic and glutamate synapse activity are increased in VPS35 D620N mutant knock-in mouse neurons, and resistant to LRRK2 kinase inhibition
Kadgien, C., Kamesh, A., & Milnerwood, A. J. (2021) · Figshare · doi:10.6084/m9.figshare.16633337
Additional file 3 of VPS35 and α-Synuclein fail to interact to modulate neurodegeneration in rodent models of Parkinson’s disease
Chen, X., Tsika, E., Levine, N. D., & Moore, D. J. (2023) · Figshare · doi:10.6084/m9.figshare.23884447
Additional file 16 of Endosomal dysfunction in iPSC-derived neural cells from Parkinson’s disease patients with VPS35 D620N
Bono, K., Hara‐Miyauchi, C., Sumi, S., Oka, H., Iguchi, Y., & Okano, H. J. (2020) · Figshare · doi:10.6084/m9.figshare.13070794
Additional file 2 of Altered striatal dopamine levels in Parkinson’s disease VPS35 D620N mutant transgenic aged mice
Vanan, S., Zeng, X., Chia, S. Y., Varnäs, K., Jiang, M., Zhang, K., Saw, W. T., Padmanabhan, P., Yu, W.-P., Zhou, Z.-D., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13317025
Additional file 4 of Endosomal dysfunction in iPSC-derived neural cells from Parkinson’s disease patients with VPS35 D620N
Bono, K., Hara‐Miyauchi, C., Sumi, S., Oka, H., Iguchi, Y., & Okano, H. J. (2020) · Figshare · doi:10.6084/m9.figshare.13071238
Additional file 2 of Endosomal dysfunction in iPSC-derived neural cells from Parkinson’s disease patients with VPS35 D620N
Bono, K., Hara‐Miyauchi, C., Sumi, S., Oka, H., Iguchi, Y., & Okano, H. J. (2020) · Figshare · doi:10.6084/m9.figshare.13071232
Additional file 14 of Endosomal dysfunction in iPSC-derived neural cells from Parkinson’s disease patients with VPS35 D620N
Bono, K., Hara‐Miyauchi, C., Sumi, S., Oka, H., Iguchi, Y., & Okano, H. J. (2020) · Figshare · doi:10.6084/m9.figshare.13070788
Additional file 1 of VPS35 and α-Synuclein fail to interact to modulate neurodegeneration in rodent models of Parkinson’s disease
Chen, X., Tsika, E., Levine, N. D., & Moore, D. J. (2023) · Figshare · doi:10.6084/m9.figshare.23884441
Additional file 2 of VPS35 and α-Synuclein fail to interact to modulate neurodegeneration in rodent models of Parkinson’s disease
Chen, X., Tsika, E., Levine, N. D., & Moore, D. J. (2023) · Figshare · doi:10.6084/m9.figshare.23884444
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Authors: Tang, F.-L., Erion, J. R., Tian, Y., Liu, W., Yin, D.-M., Ye, J., Tang, B., Mei, L., & Xiong, W.-C.
Affiliations: Augusta University (US)
Central South University (CN)
Army Medical University (CN)
ORCID: Tang, F.-L.
Tian, Y.
Liu, W.
Yin, D.-M.
Tang, B.
Mei, L.
Xiong, W.-C.
Venue: Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2015-07-22
Volume: 35
Issue: 29
Pages: 10613-10628
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.0042-15.2015
PMC: PMC4510296
OpenAlex: W1953962861
Cited by: 269
References: 55
Citations by year: 2026: 14 · 2025: 10 · 2024: 28 · 2023: 28 · 2022: 19 · 2021: 34 · 2020: 39 · 2019: 19 · 2018: 26 · 2017: 22 · 2016: 26 · 2015: 4
Type: conference abstract
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Journal of Neuroscience (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Veterans Affairs (I01 BX000838)
National Institutes of Health (AG045781)
National Institute on Aging (R01AG045781, RF1AG045781, AG045781)
National Institute of Neurological Disorders and Stroke (P30NS055077)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: VPS35, Parkinson's disease, dopaminergic neurons, LAMP2A, chaperone-mediated autophagy, alpha-synuclein degradation, retromer complex, substantia nigra pars compacta, striatum
MeSH terms: Animals, Autophagy, Cells, Cultured, Golgi Apparatus, Mice, Inbred C57BL, Mice, Mutant Strains, Endosomes, Transfection, Blotting, Western, Mutagenesis, Site-Directed, Microscopy, Confocal, Parkinsonian Disorders, Protein Transport, Vesicular Transport Proteins, Mice, alpha-Synuclein, Lysosomal-Associated Membrane Protein 2, Dopaminergic Neurons, Real-Time Polymerase Chain Reaction

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VPS35 in Dopamine Neurons Is Required for Endosome-to-Golgi Retrieval of Lamp2a, a Receptor of Chaperone-Mediated Autophagy That Is Critical for -Synuclein Degradation and Prevention of Pathogenesis of Parkinson's Disease

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