PuSH - Publikationsserver des Helmholtz Zentrums München: Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain.

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Piccoli, G. ; Onofri, F.* ; Cirnaru, M.D.* ; Kaiser, C.J.* ; Jagtap, P.K. ; Kastenmüller, A.* ; Pischedda, F.* ; Marte, A.* ; von Zweydorf, F.* ; Vogt, A. ; Giesert, F. ; Pan, L.* ; Antonucci, F.* ; Kiel, C.* ; Zhang, M.* ; Weinkauf, S.* ; Sattler, M. ; Sala, C.* ; Matteoli, M.* ; Ueffing, M. ; Gloeckner, C.J.

Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain.

Mol. Cell. Biol. 34, 2147-2161 (2014)

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Mutations in leucine-rich repeat kinase 2 gene (LRRK2) are associated with familial and sporadic Parkinson's disease (PD). LRRK2 is a complex protein that consists of multiple domains, including predicted C-terminal WD40 repeats. In this study we analyzed functional and molecular features conferred by the WD40 domain. Electron microscopic analysis of purified LRRK2 C-terminal domain revealed doughnut-shaped particles, providing experimental evidence for its WD40 fold. We demonstrate that LRRK2 WD40 binds and sequesters synaptic vesicle via interaction with vesicle-associated proteins. In fact, a domain-based pull-down approach combined with mass spectrometric analysis identified LRRK2 as being part of a highly specific protein network involved in synaptic vesicle trafficking. In addition, we found that a C-terminal sequence variant associated with an increased risk of developing PD, G2385R, correlates with a reduced binding affinity of LRRK2 WD40 to synaptic vesicles. Our data demonstrate a critical role of WD40 domain within LRRK2 function.

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