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Article

A Ubl/ubiquitin switch in the activation of Parkin

7 Aug 2015

Abstract excerpt

Mutations in Parkin and PINK1 cause an inherited early-onset form of Parkinson's disease. The two proteins function together in a mitochondrial quality control pathway whereby PINK1 accumulates on damaged mitochondria and activates Parkin to induce mitophagy. How PINK1 kinase activity releases the auto-inhibited ubiquitin ligase activity of Parkin remains unclear. Here, we identify a binding switch between...

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Identifiers

PMID: 26254305
DOI: 10.15252/embj.201592237

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Research trail→

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A Ubl/ubiquitin switch in the activation of ParkinPMID 26254305Read ↗

Structure-guided mutagenesis reveals a hierarchical mechanism of Parkin activation.Semantic proximity Read ↗

Structure of phosphorylated UBL domain and insights into PINK1-orchestrated parkin activation.Semantic proximity Read ↗

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A mechanistic review of Parkin activation.Semantic proximity Read ↗

Structure of parkin reveals mechanisms for ubiquitin ligase activation.Semantic proximity Read ↗

Structure of the human Parkin ligase domain in an autoinhibited state.Semantic proximity Read ↗

Intricate mechanism (s) of substrate specificity and loss of function on disease mutation (K211N) of ParkinSemantic proximity Read ↗

Structural basis for feedforward control in the PINK1/parkin pathwaySemantic proximity Read ↗

Structural Mechanisms of Mitochondrial Quality Control Mediated by PINK1 and ParkinSemantic proximity Read ↗

A substrate-interacting region of Parkin directs ubiquitination of the mitochondrial GTPase Miro1Semantic proximity Read ↗

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