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The unconventional G-protein cycle of LRRK2 and Roco proteins

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dc.creator Kortholt, Arjan
dc.creator Nederveen-Schippers, Laura M.
dc.creator Terheyden, Susanne
dc.date 2016-12-01T00:00:00Z
dc.date.accessioned 2023-01-09T12:09:36Z
dc.date.available 2023-01-09T12:09:36Z
dc.identifier ecf29bf3-1536-407d-b7c7-5d8b126a54d0
dc.identifier 10.1042/bst20160224
dc.identifier https://avesis.sdu.edu.tr/publication/details/ecf29bf3-1536-407d-b7c7-5d8b126a54d0/oai
dc.identifier.uri http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/98518
dc.description 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.
dc.language eng
dc.rights info:eu-repo/semantics/openAccess
dc.title The unconventional G-protein cycle of LRRK2 and Roco proteins
dc.type info:eu-repo/semantics/article


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