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Identification of potential protein interactors of Lrrk2.

ABSTRACT: Pathogenic substitutions in the Lrrk2 protein have been shown to be an important cause of both familial and sporadic parkinsonism. The molecular pathway involved in Lrrk2 dopaminergic neuron degeneration remains elusive. Employing a combination of Lrrk2-mediated protein precipitation and tandem mass spectrometry, we identified 14 potential Lrrk2 binding partners. The majority of these interactions may be subgrouped into three functional cellular pathways: (i) chaperone-mediated response, (ii) proteins associated with the cytoskeleton and trafficking and (iii) phosphorylation and kinase activity. Future investigation of these candidates is now warranted and may help resolve the pathomechanism behind Lrrk2 neurodegeneration.

SUBMITTER: Dachsel JC

PROVIDER: S-EPMC2970619 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature

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Identification of potential protein interactors of Lrrk2.

Dächsel Justus C JC Taylor Julie P JP Mok Su San SS Ross Owen A OA Hinkle Kelly M KM Bailey Rachel M RM Hines Jacob H JH Szutu Jennifer J Madden Benjamin B Petrucelli Leonard L Farrer Matthew J MJ

Parkinsonism & related disorders 20070402 7

Pathogenic substitutions in the Lrrk2 protein have been shown to be an important cause of both familial and sporadic parkinsonism. The molecular pathway involved in Lrrk2 dopaminergic neuron degeneration remains elusive. Employing a combination of Lrrk2-mediated protein precipitation and tandem mass spectrometry, we identified 14 potential Lrrk2 binding partners. The majority of these interactions may be subgrouped into three functional cellular pathways: (i) chaperone-mediated response, (ii) pr ...[more]

PMID: 17400507

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