The unconventional G-protein cycle of LRRK2 and Roco proteinsTerheyden, S., Nederveen-Schippers, L. M. & Kortholt, A., 15-Dec-2016, In : Biochemical Society Transactions. 44, 6, p. 1611-1616 6 p.
Research output: Contribution to journal › Article › Academic › peer-review
Mutations in the human leucine-rich repeat kinase 2 (LRRK2) are the most frequent cause of hereditary Parkinson's disease (PD). LRRK2 belongs to the Roco family of proteins, which are characterized by the presence of a Ras of complex proteins domain (Roc), a C-terminal of Roc domain (COR) and a kinase domain. Despite intensive research, much remains unknown about activity and the effect of PD-associated mutations. Recent biochemical and structural studies suggest that LRRK2 and Roco proteins are noncanonical G-proteins that do not depend on guanine nucleotide exchange factors or GTPase-activating proteins for activation. In this review, we will discuss the unusual G-protein cycle of LRRK2 in the context of the complex intramolecular LRRK2 activation mechanism.
|Number of pages||6|
|Journal||Biochemical Society Transactions|
|Publication status||Published - 15-Dec-2016|
- REPEAT KINASE 2, DISEASE-ASSOCIATED MUTATIONS, FAMILIAL PARKINSONS-DISEASE, GTP-BINDING, NEURONAL TOXICITY, DOMAIN, MUTANT, LEUCINE-RICH-REPEAT-KINASE-2, HYDROLYSIS, REVEALS