Samenvatting
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.
Originele taal-2 | English |
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Pagina's (van-tot) | 1611-1616 |
Aantal pagina's | 6 |
Tijdschrift | Biochemical Society Transactions |
Volume | 44 |
Nummer van het tijdschrift | 6 |
DOI's | |
Status | Published - 15-dec.-2016 |