A direct interaction between leucine-rich repeat kinase 2 and specific β-Tubulin isoforms regulates tubulin acetylation

Bernard M.H. Law, Victoria A. Spain, Veronica H.L. Leinster, Ruth Chia, Alexandra Beilina, Hyun J. Cho, Jean Marc Taymans, Mary K. Urban, Rosa M. Sancho, Marian Blanca Ramírez, Saskia Biskup, Veerle Baekelandt, Huaibin Cai, Mark R. Cookson, Daniel C. Berwick, Kirsten Harvey

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Background: Mutations in the gene encoding leucine-rich repeat kinase 2 (LRRK2) cause Parkinson disease. Results: LRRK2 binds directly to three -tubulin isoforms at the luminal face of microtubules and suppresses α-tubulin acetylation. Interaction is weakened by the R1441G LRRK2 GTPase domain mutant. Conclusion: LRRK2 modulates microtubule stability. Significance: Deregulation of microtubule-dependent processes likely contribute to neurodegeneration in Parkinson disease.

    Original languageEnglish (US)
    Pages (from-to)895-908
    Number of pages14
    JournalJournal of Biological Chemistry
    Volume289
    Issue number2
    DOIs
    StatePublished - Jan 10 2014

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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