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Cited by 1,171

The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.

PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility

Open access
Wang, Xinnan, Winter, Dominic, Ashrafi, Ghazaleh, Schlehe, Julia, Wong, Yao Liang, Selkoe, Dennis, Rice, Sarah, Steen, Judith, LaVoie, Matthew J., Schwarz, Thomas L.·2011·Cell
DOI 10.1016/j.cell.2011.10.018
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Abstract

SUMMARY Cells keep their energy balance and avoid oxidative stress by regulating mitochondrial movement, distribution, and clearance. We report here that two Parkinson’s disease proteins, the Ser/Thr-kinase PINK1 and ubiquitin-ligase Parkin, participate in this regulation by arresting mitochondrial movement. PINK1 phosphorylates Miro, a component of the primary motor/adaptor complex that anchors kinesin to the mitochondrial surface. The phosphorylation of Miro activates proteasomal degradation of Miro in a Parkin-dependent manner. Removal of Miro from the mitochondrion also detaches kinesin from its surface. By preventing mitochondrial movement, the PINK1/Parkin pathway may quarantine damaged mitochondria prior to their clearance. PINK1 has been shown to act upstream of Parkin but the mechanism corresponding to this relationship has not been known. We propose that PINK1 phosphorylation of substrates triggers the subsequent action of Parkin and the proteasome.

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Metadata

Authors
Wang, X., Winter, D., Ashrafi, G., Schlehe, J., Wong, Y. L., Selkoe, D., Rice, S., Steen, J., LaVoie, M. J., & Schwarz, T. L.
Venue
Cell
Publisher
Elsevier BV
Published
2011-11
Volume
147
Issue
4
Pages
893-906
ISSN
0092-8674 (ISSN-L)
DOI
10.1016/j.cell.2011.10.018
OpenAlex
W2149090315
Cited by
1,171
References
13
FWCI
47.93
Type
journal article
Language
en
Open access
bronze

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