Identification of potential protein interactors of Lrrk2

Justus C. Dächsel, Julie P. Taylor, Su San Mok, Owen A. Ross, Kelly M. Hinkle, Rachel M. Bailey, Jacob H. Hines, Jennifer Szutu, Benjamin Madden, Leonard Petrucelli, Matthew J. Farrer

Research output: Contribution to journalArticle

62 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)382-385
Number of pages4
JournalParkinsonism and Related Disorders
Volume13
Issue number7
DOIs
StatePublished - Oct 1 2007
Externally publishedYes

Keywords

  • Interactors
  • Lrrk2
  • Tandem mass spectrometry

ASJC Scopus subject areas

  • Neurology
  • Geriatrics and Gerontology
  • Clinical Neurology

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  • Cite this

    Dächsel, J. C., Taylor, J. P., Mok, S. S., Ross, O. A., Hinkle, K. M., Bailey, R. M., Hines, J. H., Szutu, J., Madden, B., Petrucelli, L., & Farrer, M. J. (2007). Identification of potential protein interactors of Lrrk2. Parkinsonism and Related Disorders, 13(7), 382-385. https://doi.org/10.1016/j.parkreldis.2007.01.008