The unconventional G-protein cycle of LRRK2 and Roco proteins
BIOCHEMICAL SOCIETY TRANSACTIONS, cilt.44, ss.1611-1616, 2016 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Derleme
- Cilt numarası: 44
- Basım Tarihi: 2016
- Doi Numarası: 10.1042/bst20160224
- Dergi Adı: BIOCHEMICAL SOCIETY TRANSACTIONS
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.1611-1616
- Açık Arşiv Koleksiyonu: AVESİS Açık Erişim Koleksiyonu
- Süleyman Demirel Üniversitesi Adresli: Hayır
Özet
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.