ParkinsonCanadaV1, France, Analysis, bibRecord, 000229

Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

Identifieur interne : 000229 ( France/Analysis ); précédent : 000228; suivant : 000230

Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

Auteurs : Monica Joch ; Ariel R. Ase [Canada] ; Carol X.-Q. Chen ; Penny A. Macdonald ; Maria Kontogiannea ; Amadou T. Corera ; Alexis Brice [France] ; Philippe Séguéla [Canada] ; Edward A. Fon

Source :

Molecular Biology of the Cell [ 1059-1524 ] ; 2007.

RBID : PMC:1949385

Abstract

Mutations in the parkin gene result in an autosomal recessive juvenile-onset form of Parkinson's disease. As an E3 ubiquitin-ligase, parkin promotes the attachment of ubiquitin onto specific substrate proteins. Defects in the ubiquitination of parkin substrates are therefore believed to lead to neurodegeneration in Parkinson's disease. Here, we identify the PSD-95/Discs-large/Zona Occludens-1 (PDZ) protein PICK1 as a novel parkin substrate. We find that parkin binds PICK1 via a PDZ-mediated interaction, which predominantly promotes PICK1 monoubiquitination rather than polyubiquitination. Consistent with monoubiquitination and recent work implicating parkin in proteasome-independent pathways, parkin does not promote PICK1 degradation. However, parkin regulates the effects of PICK1 on one of its other PDZ partners, the acid-sensing ion channel (ASIC). Overexpression of wild-type, but not PDZ binding– or E3 ubiquitin-ligase–defective parkin abolishes the previously described, protein kinase C-induced, PICK1-dependent potentiation of ASIC2a currents in non-neuronal cells. Conversely, the loss of parkin in hippocampal neurons from parkin knockout mice unmasks prominent potentiation of native ASIC currents, which is normally suppressed by endogenous parkin in wild-type neurons. Given that ASIC channels contribute to excitotoxicity, our work provides a mechanism explaining how defects in parkin-mediated PICK1 monoubiquitination could enhance ASIC activity and thereby promote neurodegeneration in Parkinson's disease.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1949385

DOI: 10.1091/mbc.E05-11-1027
PubMed: 17553932
PubMed Central: 1949385

Affiliations:

Links to Exploration step

PMC:1949385

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p>Mutations in the <italic>parkin</italic>
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La maladie de Parkinson au Canada (serveur d'exploration)

Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

Source :

Abstract

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Links to Exploration step

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Pour générer des pages wiki

	La maladie de Parkinson au Canada (serveur d'exploration)
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