The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Regulation of ER-mitochondria contacts by Parkin via Mfn2
Open accessAbstract
Parkin, an E3 ubiquitin ligase and a Parkinson’s disease (PD) related gene, translocates to impaired mitochondria and drives their elimination via autophagy, a process known as mitophagy. Mitochondrial pro-fusion protein Mitofusins (Mfn1 and Mfn2) were found to be a target for Parkin mediated ubiquitination. Mfns are transmembrane GTPase embedded in the outer membrane of mitochondria, which are required on adjacent mitochondria to mediate fusion. In mammals, Mfn2 also forms complexes that are capable of tethering mitochondria to endoplasmic reticulum (ER), a structural feature essential for mitochondrial energy metabolism, calcium (Ca2+) transfer between the organelles and Ca2+ dependent cell death. Despite its fundamental physiological role, the molecular mechanisms that control ER-mitochondria cross talk are obscure. Ubiquitination has recently emerged as a powerful tool to modulate protein function, via regulation of protein subcellular localization and protein ability to interact with other proteins. Ubiquitination is also a reversible mechanism, which can be actively controlled by opposing ubiquitination-deubiquitination events. In this work we found that in Parkin deficient cells and parkin mutant human fibroblasts, the tether between ER and mitochondria is decreased. We identified the site of Parkin dependent ubiquitination and showed that the non-ubiquitinatable Mfn2 mutant fails to restore ER-mitochondria physical and functional interaction. Finally, we took advantage of an established in vivo model of PD to demonstrate that manipulation of ER-mitochondria tethering by expressing an ER-mitochondria synthetic linker is sufficient to rescue the locomotor deficit associated to an in vivo Drosophila model of PD.
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Citations
Cites
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
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PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
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Mitofusin 2 tethers endoplasmic reticulum to mitochondria
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Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
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Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
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Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
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Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
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Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
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“A similar pattern of ubiquitination was also previously described for Mfn2 in Hela cells [21], human neuroblastoma cells SH-SY5Y [22] and for the yeast Mfn homologue, Fig.”
InfluentialOPA1 requires mitofusin 1 to promote mitochondrial fusion
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Wang, X., Li, Y., He, M., Kong, X., Jiang, P., Liu, X., Diao, L., Zhang, X., Li, H., Ling, X., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab962 · Cited by 260
Mitophagy in Acute Kidney Injury and Kidney Repair
Wang, Y., Cai, J., Tang, C., & Dong, Z. (2020) · Cells · doi:10.3390/cells9020338 · Cited by 130
Larsen, T. D., Sabey, K. H., Knutson, A. J., Gandy, T. C. T., Louwagie, E. J., Lauterboeck, L., Mdaki, K. S., & Baack, M. L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20123090 · Cited by 57
Lin, T.-K., Lin, K.-J., Lin, K.-L., Liou, C.-W., Chen, S.-D., Chuang, Y.-C., Wang, P.-W., Chuang, J.-H., & Wang, T.-J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607392 · Cited by 19
Metadata
- Authors
- Basso, V., Marchesan, E., Peggion, C., Chakraborty, J., von Stockum, S., Giacomello, M., Ottolini, D., Debattisti, V., Caicci, F., Tasca, E., Pegoraro, V., Angelini, C., Antonini, A., Bertoli, A., Brini, M., & Ziviani, E.
- Venue
- Pharmacological Research
- Publisher
- Elsevier BV
- Published
- 2018-12
- Volume
- 138
- Pages
- 43-56
- ISSN
- 1043-6618 (ISSN-L)
- OpenAlex
- W2891311921
- Cited by
- 207
- References
- 24
- FWCI
- 13.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Basso, V., Marchesan, E., Peggion, C., Chakraborty, J., von Stockum, S., Giacomello, M., Ottolini, D., Debattisti, V., Caicci, F., Tasca, E., Pegoraro, V., Angelini, C., Antonini, A., Bertoli, A., Brini, M., & Ziviani, E. (2018). Regulation of ER-mitochondria contacts by Parkin via Mfn2. Pharmacological Research. https://doi.org/10.1016/j.phrs.2018.09.006
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