The mouse/human cross-species heterodimer of leucine-rich repeat kinase 2: Possible significance in the transgenic model mouse of Parkinson's disease

Neuroscience Letters

Volumn 588, Issue , 2015, Pages 142-146

  Miyajima, T ^a   Ohta, E ^a,b   Kawada, H ^a   Maekawa, T ^a,b   Obata, F ^a,b  

^a KITASATO UNIVERSITY GRADUATE SCHOOL OF MEDICAL SCIENCES   (Japan)

^b KITASATO UNIVERSITY   (Japan)

Author keywords

Cross species heterodimer; Intracellular degradation; Leucine rich repeat kinase 2 (LRRK2); Parkinson's disease; Transgenic mouse

Indexed keywords

HETERODIMER; LEUCINE RICH REPEAT KINASE 2; LRRK2 PROTEIN, HUMAN; LRRK2 PROTEIN, MOUSE; PROTEIN SERINE THREONINE KINASE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BRAIN; CELL LYSATE; CONTROLLED STUDY; GEL ELECTROPHORESIS; GENE EXPRESSION; GENETIC TRANSFECTION; HEK293 CELL LINE; HUMAN; IMMUNOPRECIPITATION; MOLECULAR WEIGHT; MOUSE; NEUROBLASTOMA; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; ANIMAL; DISEASE MODEL; GENETICS; METABOLISM; MUTATION; PROTEIN MULTIMERIZATION; TRANSGENIC MOUSE;

ANIMALS; DISEASE MODELS, ANIMAL; HEK293 CELLS; HUMANS; MICE; MICE, TRANSGENIC; MUTATION; PARKINSON DISEASE; PROTEIN MULTIMERIZATION; PROTEIN-SERINE-THREONINE KINASES;

EID: 84923035922     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2015.01.003     Document Type: Article

References (21)

1. Paisan-Ruiz C., Jain S., Evans E.W., et al. Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease. Neuron 2004, 44:595-600.
2. Zimprich A., Biskup S., Leitner P., et al. Mutations in LRRK2 cause autosomaldominant Parkinsonism with pleomorphic pathology. Neuron 2004, 44:601-607.
3. Funayama M., Hasegawa K., Ohta E., et al. An LRRK2 mutation as a cause for the Parkinsonism in the original PARK8 family. Ann. Neurol. 2005, 57:918-921.
4. Meylan E., Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci. 2005, 30:151-159.
5. Sen S., Webber P.J., West A.B. Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization. J. Biol. Chem. 2009, 284:36346-36356.
6. Greggio E., Zambrano I., Kaganovich A., et al. The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation. J. Biol. Chem. 2008, 283:16906-16914.
7. Ohta E., Katayama Y., Kawakami F., et al. I2020T leucine-rich repeat kinase 2, the causative mutant molecule of familial Parkinson's disease, has a higherintracellular degradation rate than the wild-type molecule. Biochem. Biophys. Res. Commun. 2009, 390:710-715.
8. Ohta E., Kubo M., Obata F. Prevention of intracellular degradation of I2020T mutant LRRK2 restores its protectivity against apoptosis. Biochem. Biophys. Res. Commun. 2010, 391:242-247.
9. Ohta E., Kawakami F., Kubo M., Obata F. Dominant-negative effects of LRRK2 heterodimers: a possible mechanism of neurodegeneration in Parkinson's disease caused by LRRK2 I2020T mutation. Biochem. Biophys. Res. Commun. 2013, 430:560-566.
10. Maekawa T., Mori S., Sasaki T., et al. The I2020T Leucine-rich repeat kinase 2 transgenic mouse exhibits impaired locomotive ability accompanied by dopaminergic neuron abnormalities. Mol. Neurodegener. 2012, 10.1186/1750-1326-7-15.
11. Biskup S., Moore D.J., Rea A., et B. Dynamic and redundant regulation of LRRK2 and LRRK1 expression. BMC Neurosci. 2007, 10.1186/1471-2202-8-102.
12. Klein C.L., Rovelli G., Springer W., et al. Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. 2009, 111:703-715.
13. Dachsel J.C., Nishioka K., Vilariño-Güell C., et al. Heterodimerization of Lrrk1-Lrrk2: implications for LRRK2-associated Parkinson disease 2010, 131:210-214.
14. Jaleel M., Nichols R.J., Deak M., et al. LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. Biochem. J. 2007, 405:307-317.
15. Gandhi P.N., Wang X., Zhu X., et al. The ROC domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules. J. Neurosci. Res. 2008, 86:1711-1720.
16. Narae S., Hyerhan J., Jungsun K., et al. LRRK2 regulates synaptic vesicle endocytosis. Exp. Cell Res. 2008, 314:2055-2065.
17. Imai Y., Gehrke S., Wang H.Q., et al. Phosphorylation of 4E-BP by LRRK2 affectsthe maintenance of dopaminergic neurons in drosophila. EMBO J. 2008, 27:2432-2443.
18. Hsu C.H., Chan D., Greggio E., et al. MKK6 binds and regulates expression of Parkinson's disease-related protein LRRK2. J. Neurochem. 2010, 112:1593-1604.
19. Ohta E., Kawakami F., Kubo M., Obata F. LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutations. FEBS Lett. 2011, 585:2165-2170.
20. Lichtenberg A., et al. The Parkinson's disease protein LRRK2 impairs proteasome substrate clearance without affecting proteasome catalytic activity. Cell Death Dis. 2011, e196. 10.1038/cddis.2011.81.
21. Kawakami T., et al. LRRK2 phosphorylates tubulin-associated tau but not the free molecule: possible LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowth. ProS ONE 2012, 7:e30834. 10.1371/journal.pone.0030834.