Titlebook: Leucine-Rich Repeat Kinase 2 (LRRK2); Hardy J. Rideout Book 2017 Springer International Publishing AG 2017 GTPase.Parkinson‘s Disease.kina

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978-3-319-84287-5Springer International Publishing AG 2017

Compassionate

Leucine-Rich Repeat Kinase 2 (LRRK2)978-3-319-49969-7Series ISSN 2190-5215 Series E-ISSN 2190-5223

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Hardy J. RideoutThorough overview of the current state of knowledge on LRRK2.Discussed the links between LRRK2 mutations and Parkinson‘s Disease.Explores what we know about the normal function of LRRK2.Includes suppl

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Advances in Neurobiologyhttp://image.papertrans.cn/l/image/585293.jpg

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Clinical Features of , Carriers with Parkinson’s Diseaseciated with PD, the most common of which is the Gly2019Ser mutation. In the following review, we summarize the demographics and motor and non-motor symptoms of . carriers with PD, as well as symptoms in non-manifesting carriers. The clinical features of .-associated PD are often indistinguishable fr

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LRRK2 Phosphorylationnson’s disease. LRRK2 is a large multi-domain protein with a functional GTPase and kinase domain. The signal transduction pathways in which LRRK2 is dysfunctional in the disease state are only now being resolved, but we do know that LRRK2 is, itself, a substrate of multiple kinases and phosphatases

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Understanding the GTPase Activity of LRRK2: Regulation, Function, and Neurotoxicityto the ROCO superfamily of proteins, characterized by a Ras-of-complex (Roc) GTPase domain in tandem with a C-terminal-of-Roc (COR) domain. LRRK2 also contains a protein kinase domain adjacent to the Roc-COR tandem domain in addition to multiple repeat domains. Disease-causing familial mutations clu

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LRRK2 and Autophagyd as autophagy. In this chapter, the evidence linking LRRK2 to autophagy will be examined, along with how regulation of autophagy and lysosomal pathways may provide a nexus between the physiological function of this protein and the different diseases with which it has been associated. Data from cell