The LRRK2 G2385R variant is a partial loss-of-function mutation that affects synaptic vesicle trafficking through altered protein interactions

[1]  John Hardy,et al.  199 years of Parkinson disease – what have we learned and what is the path to the future? , 2016, Journal of neurochemistry.

[2]  M. Ueffing,et al.  Structural model of the dimeric Parkinson’s protein LRRK2 reveals a compact architecture involving distant interdomain contacts , 2016, Proceedings of the National Academy of Sciences.

[3]  W. Seol,et al.  G2385R and I2020T Mutations Increase LRRK2 GTPase Activity , 2016, BioMed research international.

[4]  G. Piccoli,et al.  LRRK2 Regulates Voltage-Gated Calcium Channel Function , 2016, Front. Mol. Neurosci..

[5]  Andrew B Singleton,et al.  Genetics in Parkinson disease: Mendelian versus non‐Mendelian inheritance , 2016, Journal of neurochemistry.

[6]  L. Bubacco,et al.  LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate , 2016, Molecular Neurodegeneration.

[7]  C. Perego,et al.  TIRFM and pH-sensitive GFP-probes to evaluate neurotransmitter vesicle dynamics in SH-SY5Y neuroblastoma cells: cell imaging and data analysis. , 2015, Journal of visualized experiments : JoVE.

[8]  I. Martin,et al.  LRRK2 pathobiology in Parkinson's disease , 2014, Journal of neurochemistry.

[9]  Marco Y. Hein,et al.  Accurate Protein Complex Retrieval by Affinity Enrichment Mass Spectrometry (AE-MS) Rather than Affinity Purification Mass Spectrometry (AP-MS)* , 2014, Molecular & Cellular Proteomics.

[10]  N. Kuhlmann,et al.  Synaptic function is modulated by LRRK2 and glutamate release is increased in cortical neurons of G2019S LRRK2 knock-in mice , 2014, Front. Cell. Neurosci..

[11]  L. Civiero,et al.  Genetic, Structural, and Molecular Insights into the Function of Ras of Complex Proteins Domains , 2014, Chemistry & biology.

[12]  J. Gan,et al.  The association between the LRRK2 G2385R variant and the risk of Parkinson’s disease: a meta-analysis based on 23 case–control studies , 2014, Neurological Sciences.

[13]  Marco Y. Hein,et al.  Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ * , 2014, Molecular & Cellular Proteomics.

[14]  E. Fedele,et al.  LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex , 2014, Front. Mol. Neurosci..

[15]  C. Kiel,et al.  Leucine-Rich Repeat Kinase 2 Binds to Neuronal Vesicles through Protein Interactions Mediated by Its C-Terminal WD40 Domain , 2014, Molecular and Cellular Biology.

[16]  S. Rizzoli.  Synaptic vesicle recycling: steps and principles , 2014, The EMBO journal.

[17]  M. Francolini,et al.  A Cell Surface Biotinylation Assay to Reveal Membrane-associated Neuronal Cues: Negr1 Regulates Dendritic Arborization* , 2013, Molecular & Cellular Proteomics.

[18]  T. Südhof,et al.  The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices--guilty as charged? , 2012, Annual review of cell and developmental biology.

[19]  Heung-Chin Cheng,et al.  Analysis of LRRK2 accessory repeat domains: prediction of repeat length, number and sites of Parkinson's disease mutations. , 2012, Biochemical Society transactions.

[20]  P. Verstreken,et al.  LRRK2 Controls an EndoA Phosphorylation Cycle in Synaptic Endocytosis , 2012, Neuron.

[21]  M. Cookson,et al.  Biochemical Characterization of Highly Purified Leucine-Rich Repeat Kinases 1 and 2 Demonstrates Formation of Homodimers , 2012, PloS one.

[22]  M. Cookson,et al.  The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation. , 2012, The Biochemical journal.

[23]  Hitoshi Takahashi,et al.  The Lewy Body in Parkinson’s Disease and Related Neurodegenerative Disorders , 2012, Molecular Neurobiology.

[24]  K. Staras,et al.  Synapsin Selectively Controls the Mobility of Resting Pool Vesicles at Hippocampal Terminals , 2012, The Journal of Neuroscience.

[25]  W. Wurst,et al.  LRRK2 Controls Synaptic Vesicle Storage and Mobilization within the Recycling Pool , 2011, The Journal of Neuroscience.

[26]  E. Marcotte,et al.  It's the machine that matters: Predicting gene function and phenotype from protein networks. , 2010, Journal of proteomics.

[27]  A. Prescott,et al.  14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization , 2010, The Biochemical journal.

[28]  F. Benfenati,et al.  Tyrosine phosphorylation of synapsin I by Src regulates synaptic-vesicle trafficking , 2010, Journal of Cell Science.

[29]  Z. Berger,et al.  Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation. , 2010, Biochemistry.

[30]  J. Buxbaum,et al.  Enhanced Striatal Dopamine Transmission and Motor Performance with LRRK2 Overexpression in Mice Is Eliminated by Familial Parkinson's Disease Mutation G2019S , 2010, The Journal of Neuroscience.

[31]  Yih-Ru Wu,et al.  LRRK2 G2385R modulates age at onset in Parkinson's disease: A multi‐center pooled analysis , 2009, American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics.

[32]  A. Pisani,et al.  R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice , 2009, Proceedings of the National Academy of Sciences.

[33]  T. Südhof,et al.  SV2 Renders Primed Synaptic Vesicles Competent for Ca2+-Induced Exocytosis , 2009, The Journal of Neuroscience.

[34]  E. Kremmer,et al.  Generation and characterization of a rat monoclonal antibody specific for multiple red fluorescent proteins. , 2008, Hybridoma.

[35]  M. Cookson,et al.  The Parkinson Disease-associated Leucine-rich Repeat Kinase 2 (LRRK2) Is a Dimer That Undergoes Intramolecular Autophosphorylation* , 2008, Journal of Biological Chemistry.

[36]  S. Hilfiker,et al.  Vesicle pools and synapsins: New insights into old enigmas , 2007, Brain cell biology.

[37]  E. Tan.  Identification of a common genetic risk variant (LRRK2 Gly2385Arg) in Parkinson's disease. , 2006, Annals of the Academy of Medicine, Singapore.

[38]  Leon Lagnado,et al.  Clathrin-Mediated Endocytosis Is the Dominant Mechanism of Vesicle Retrieval at Hippocampal Synapses , 2006, Neuron.

[39]  T. Meitinger,et al.  The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. , 2006, Human molecular genetics.

[40]  Yuval Garini,et al.  From micro to nano: recent advances in high-resolution microscopy. , 2005, Current opinion in biotechnology.

[41]  L H Schaefer,et al.  Structured illumination microscopy: artefact analysis and reduction utilizing a parameter optimization approach , 2004, Journal of microscopy.

[42]  J. Noebels,et al.  Presynaptic Ca2+ Channels and Neurotransmitter Release at the Terminal of a Mouse Cortical Neuron , 2001, The Journal of Neuroscience.

[43]  T. Sejnowski,et al.  Heterogeneous Release Properties of Visualized Individual Hippocampal Synapses , 1997, Neuron.

[44]  F Benfenati,et al.  Synaptic vesicle phosphoproteins and regulation of synaptic function. , 1993, Science.

[45]  P. Greengard,et al.  Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation , 1983, The Journal of cell biology.

[46]  A. West,et al.  14-3-3 Proteins regulate mutant LRRK2 kinase activity and neurite shortening. , 2016, Human molecular genetics.

[47]  M. Santos‐Reis,et al.  Competing interests , 2010 .

[48]  E. Kremmer,et al.  Prevention of interferon-stimulated gene expression using microRNA-designed hairpins , 2009, Gene Therapy.