Cited by 440Parkinson's Disease Mechanisms and TreatmentsMitochondrial Function and PathologyAutophagy in Disease and Therapy

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The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway

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Poole, Angela C., Thomas, Ruth E., Yu, Selina, Vincow, Evelyn S., Pallanck, Leo·2010·PLoS ONE

DOI 10.1371/journal.pone.0010054PMC PMC2850930

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Abstract

Loss-of-function mutations in the PINK1 or parkin genes result in recessive heritable forms of parkinsonism. Genetic studies of Drosophila orthologs of PINK1 and parkin indicate that PINK1, a mitochondrially targeted serine/threonine kinase, acts upstream of Parkin, a cytosolic ubiquitin-protein ligase, to promote mitochondrial fragmentation, although the molecular mechanisms by which the PINK1/Parkin pathway promotes mitochondrial fragmentation are unknown. We tested the hypothesis that PINK1 and Parkin promote mitochondrial fragmentation by targeting core components of the mitochondrial morphogenesis machinery for ubiquitination. We report that the steady-state abundance of the mitochondrial fusion-promoting factor Mitofusin (dMfn) is inversely correlated with the activity of PINK1 and Parkin in Drosophila. We further report that dMfn is ubiquitinated in a PINK1- and Parkin-dependent fashion and that dMfn co-immunoprecipitates with Parkin. By contrast, perturbations of PINK1 or Parkin did not influence the steady-state abundance of the mitochondrial fission-promoting factor Drp1 or the mitochondrial fusion-promoting factor Opa1, or the subcellular distribution of Drp1. Our findings suggest that dMfn is a direct substrate of the PINK1/Parkin pathway and that the mitochondrial morphological alterations and tissue degeneration phenotypes that derive from mutations in PINK1 and parkin result at least in part from reduced ubiquitin-mediated turnover of dMfn.

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Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705
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Additional file 3 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
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Additional file 13 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
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Additional file 6 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
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Additional file 7 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062331
Additional file 15 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062268
Additional file 16 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
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Additional file 11 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062229
Additional file 14 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062253
Additional file 9 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062343
Additional file 8 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062337
Additional file 1 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062292
Additional file 10 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062223
Additional file 2 of PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Figshare · doi:10.6084/m9.figshare.12062298
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Authors: Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., & Pallanck, L.
Affiliations: University of Washington (US)
Corresponding author: Pallanck, Leo
ORCID: Poole, Angela C.
Thomas, Ruth E.
Yu, Selina
Vincow, Evelyn S.
Pallanck, Leo
Venue: PLoS ONE
Publisher: Public Library of Science (PLoS)
Published: 2010-04-07
Volume: 5
Issue: 4
Pages: e10054
ISSN: 1932-6203 (ISSN-L)
DOI: 10.1371/journal.pone.0010054
PMC: PMC2850930
OpenAlex: W2054556550
Cited by: 440
References: 41
Citations by year: 2026: 4 · 2025: 4 · 2024: 17 · 2023: 14 · 2022: 13 · 2021: 26 · 2020: 35 · 2019: 16 · 2018: 26 · 2017: 27 · 2016: 30 · 2015: 39 · 2014: 38 · 2013: 44 · 2012: 54
FWCI: 28.77
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (unspecified)
Locations: PLoS ONE (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders: National Institutes of Health
National Institute on Aging (T32AG000057)
National Institute of General Medical Sciences (R01GM086394)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: mitofusins, PINK1, Parkin, PINK1/Parkin pathway, mitochondrial fusion, mitochondrial fragmentation, ubiquitination, parkinsonism, Drp1, OPA1, Drosophila, mitochondrial morphogenesis
MeSH terms: PTEN-Induced Putative Kinase, Membrane Proteins, Mitochondria, Mutation, Protein Serine-Threonine Kinases, Drosophila Proteins, Ubiquitin-Protein Ligases, Immunoprecipitation, Ubiquitination, Protein Stability

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The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway

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