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LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex

Cirnaru, Maria D., Marte, Antonella, Belluzzi, Elisa, Russo, Isabella, Gabrielli, Martina, Longo, Francesco, Arcuri, Ludovico, Murru, Luca, Bubacco, Luigi, Matteoli, Michela, Fedele, Ernesto, Sala, Carlo, Passafaro, Maria, Morari, Michele, Greggio, Elisa, Onofri, Franco, Piccoli, Giovanni·2014·Frontiers in Molecular Neuroscience

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Research works printed but not linked: 52

  1. Aasly, 2005, Clinical features of LRRK2-associated Parkinson's disease in central Norway, Ann. Neurol, 57, 762, 10.1002/ana.20456 · DOI
  2. Bauer, 2009, Prevention of interferon-stimulated gene expression using microRNA-designed hairpins, Gene Ther, 16, 142, 10.1038/gt.2008.123 · DOI
  3. Belluzzi, 2012, Presynaptic dysfunction in Parkinson's disease: a focus on LRRK2, Biochem. Soc. Trans, 40, 1111, 10.1042/BST20120124 · DOI
  4. Berg, 2005, Type and frequency of mutations in the LRRK2 gene in familial and sporadic Parkinson's disease*, Brain, 128, 3000, 10.1093/brain/awh666 · DOI
  5. Berger, 2010, Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation, Biochemistry, 49, 5511, 10.1021/bi100157u · DOI
  6. Bosgraaf, 2003, Roc, a Ras/GTPase domain in complex proteins, Biochim. Biophys. Acta, 1643, 5, 10.1016/j.bbamcr.2003.08.008 · DOI
  7. Brice, 2005, Genetics of Parkinson's disease: LRRK2 on the rise, Brain, 128, 8475, 10.1093/brain/awh676 · DOI
  8. Civiero, 2012, Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers, PLoS ONE, 7, e43472, 10.1371/journal.pone.0043472 · DOI
  9. Deng, 2008, Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase, Proc. Natl. Acad. Sci. U.S.A, 105, 1499, 10.1073/pnas.0709098105 · DOI
  10. Deng, 2011, Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2, Nat. Chem. Biol, 7, 203, 10.1038/nchembio.538 · DOI
  11. Gillardon, 2013, ATP-competitive LRRK2 inhibitors interfere with monoclonal antibody binding to the kinase domain of LRRK2 under native conditions. A method to directly monitor the active conformation of LRRK2?, J. Neurosci. Methods, 214, 62, 10.1016/j.jneumeth.2012.12.015 · DOI
  12. Gloeckner, 2006, The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity, Hum. Mol. Genet, 15, 223, 10.1093/hmg/ddi439 · DOI
  13. Greengard, 1993, Synaptic vesicle phosphoproteins and regulation of synaptic function, Science, 259, 780, 10.1126/science.8430330 · DOI
  14. Greggio, 2006, Kinase activity is required for the toxic effects of mutant LRRK2/dardarin, Neurobiol. Dis, 23, 329, 10.1016/j.nbd.2006.04.001 · DOI · Paper page
  15. Greggio, 2008, The Parkinson disease-associated leucine-rich repeat Kinase 2 (LRRK2) Is a dimer that undergoes intramolecular autophosphorylation, J. Biol. Chem, 283, 16906, 10.1074/jbc.M708718200 · DOI
  16. Guo, 2006, Leucine-rich repeat kinase 2: relevance to Parkinson's disease, Int. J. Biochem. Cell Biol, 38, 1469, 10.1016/j.biocel.2006.02.009 · DOI
  17. Hardy, 2006, Genetics of Parkinson's disease and parkinsonism, Ann. Neurol, 60, 389, 10.1002/ana.21022 · DOI
  18. Herzig, 2011, LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice, Hum. Mol. Genet, 20, 4209, 10.1093/hmg/ddr348 · DOI
  19. Hinkle, 2012, LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors, Mol. Neurodegener, 7, 25, 10.1186/1750-1326-7-25 · DOI
  20. Huttner, 1983, Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation, J. Cell Biol, 96, 1374, 10.1083/jcb.96.5.1374 · DOI
  21. Ito, 2012, Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form, Biochem. J, 441, 987, 10.1042/BJ20111215 · DOI
  22. Klein, 2009, Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment, J. Neurochem, 111, 703, 10.1111/j.1471-4159.2009.06358.x · DOI
  23. Laemmli, 1970, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, 227, 680, 10.1038/227680a0 · DOI · Paper page
  24. Li, 2010, Enhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019S, J. Neurosci, 30, 1788, 10.1523/JNEUROSCI.5604-09.2010 · DOI
  25. Luerman, 2014, Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN-1, J. Neurochem, 128, 561, 10.1111/jnc.12483 · DOI
  26. MacLeod, 2006, The familial Parkinsonism gene LRRK2 regulates neurite process morphology, Neuron, 52, 587, 10.1016/j.neuron.2006.10.008 · DOI
  27. Marte, 2010, Alterations of glutamate release in the spinal cord of mice with experimental autoimmune encephalomyelitis, J. Neurochem, 115, 343, 10.1111/j.1471-4159.2010.06923.x · DOI
  28. Marti, 2003, Plasticity of glutamatergic control of striatal acetylcholine release in experimental parkinsonism: opposite changes at group-II metabotropic and NMDA receptors, J. Neurochem, 84, 792, 10.1046/j.1471-4159.2003.01569.x · DOI
  29. Matta, 2012, LRRK2 controls an EndoA phosphorylation cycle in synaptic endocytosis, Neuron, 75, 1008, 10.1016/j.neuron.2012.08.022 · DOI · Paper page
  30. Matteoli, 1992, Exo-endocytotic recycling of synaptic vesicles in developing processes of cultured hippocampal neurons, J. Cell Biol, 117, 849, 10.1083/jcb.117.4.849 · DOI
  31. Mela, 2004, Pharmacological profile of nociceptin/orphanin FQ receptors regulating 5-hydroxytryptamine release in the mouse neocortex, Eur. J. Neurosci, 19, 1317, 10.1111/j.1460-9568.2004.03220.x · DOI
  32. Melrose, 2010, Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice, Neurobiol. Dis, 40, 503, 10.1016/j.nbd.2010.07.010 · DOI
  33. Messa, 2010, Tyrosine phosphorylation of synapsin I by Src regulates synaptic-vesicle trafficking, J. Cell Sci, 123, 2256, 10.1242/jcs.068445 · DOI
  34. Migheli, 2013, LRRK2 affects vesicle trafficking, neurotransmitter extracellular level and membrane receptor localization, PLoS ONE, 8, e77198, 10.1371/journal.pone.0077198 · DOI
  35. Moore, 2005, Molecular pathophysiology of Parkinson's disease, Annu. Rev. Neurosci, 28, 57, 10.1146/annurev.neuro.28.061604.135718 · DOI
  36. Nichols, 2009, Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease, Biochem. J, 424, 47, 10.1042/BJ20091035 · DOI
  37. Nichols, 2010, 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization, Biochem. J, 430, 393, 10.1042/BJ20100483 · DOI
  38. Onofri, 2007, Synapsin phosphorylation by SRC tyrosine kinase enhances SRC activity in synaptic vesicles, J. Biol. Chem, 282, 15754, 10.1074/jbc.M701051200 · DOI
  39. Orenbuch, 2012, Synapsin selectively controls the mobility of resting pool vesicles at hippocampal terminals, J. Neurosci, 32, 3969, 10.1523/JNEUROSCI.5058-11.2012 · DOI
  40. Paisan-Ruiz, 2004, Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease, Neuron, 44, 595, 10.1016/j.neuron.2004.10.023 · DOI
  41. Piccoli, 2011, LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool, J. Neurosci, 31, 2225, 10.1523/JNEUROSCI.3730-10.2011 · DOI
  42. Piccoli, 2014, LRRK2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain, Mol. Cell. Biol, 10.1128/MCB.00914-13 · DOI · Paper page
  43. Piccoli, 2007, Proteomic analysis of activity-dependent synaptic plasticity in hippocampal neurons, J. Proteome Res, 6, 3203, 10.1021/pr0701308 · DOI
  44. Reith, 2012, GSK2578215A; a potent and highly selective 2-arylmethyloxy-5-substitutent-N-arylbenzamide LRRK2 kinase inhibitor, Bioorg. Med. Chem. Lett, 22, 5625, 10.1016/j.bmcl.2012.06.104 · DOI
  45. Sen, 2009, Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization, J. Biol, 284, 36346, 10.1074/jbc.M109.025437 · DOI
  46. Sheng, 2012, Ser1292 autophosphorylation is an indicator of LRRK2 kinase activity and contributes to the cellular effects of PD mutations, Sci. Transl. Med, 4, 164ra161, 10.1126/scitranslmed.3004485 · DOI
  47. Shin, 2008, LRRK2 regulates synaptic vesicle endocytosis, Exp. Cell Res, 314, 2055, 10.1016/j.yexcr.2008.02.015 · DOI
  48. Tong, 2009, R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice, Proc. Natl. Acad. Sci. U.S.A, 106, 14622, 10.1073/pnas.0906334106 · DOI
  49. Verderio, 1999, Internalization and proteolytic action of botulinum toxins in CNS neurons and astrocytes, J. Neurochem, 73, 372, 10.1046/j.1471-4159.1999.0730372.x · DOI
  50. West, 2005, Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity, Proc. Natl. Acad. Sci. U.S.A, 102, 16842, 10.1073/pnas.0507360102 · DOI · Paper page
  51. Yun, 2013, LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25, Exp. Mol. Med, 45, e36, 10.1038/emm.2013.68 · DOI
  52. Zimprich, 2004, Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology, Neuron, 44, 601, 10.1016/j.neuron.2004.11.005 · DOI

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Authors
Cirnaru, M. D., Marte, A., Belluzzi, E., Russo, I., Gabrielli, M., Longo, F., Arcuri, L., Murru, L., Bubacco, L., Matteoli, M., Fedele, E., Sala, C., Passafaro, M., Morari, M., Greggio, E., Onofri, F., & Piccoli, G.
Venue
Frontiers in Molecular Neuroscience
Published
2014-05-27
Volume
7
ISSN
1662-5099
Cited by
93
References
0

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