Interferon-γ induces leucine-rich repeat kinase LRRK2 via extracellular signal-regulated kinase ERK5 in macrophages

Journal of Neurochemistry

Volumn 129, Issue 6, 2014, Pages 980-987

  Kuss, Martin ^a,b   Adamopoulou, Eleni ^a   Kahle, Philipp J ^a,b,c  

^a UNIVERSITY OF TÜBINGEN   (Germany)

^b GERMAN CENTER FOR NEURODEGENERATIVE DISEASES DZNE   (Germany)

^c UNIVERSITY OF TÜBINGEN   (Germany)

Author keywords

extracellular signal regulated kinase; interferon; leucine rich repeat kinase; macrophages; mitogen Activated protein kinase; signal transduction

Indexed keywords

GAMMA INTERFERON; LEUCINE RICH REPEAT KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE 7;

ACUTE MONOCYTIC LEUKEMIA; ARTICLE; CELL DIFFERENTIATION; CELL STIMULATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INDUCTION; ENZYME INHIBITION; HUMAN; HUMAN CELL; IMMUNOHISTOCHEMISTRY; LEUKEMIA CELL LINE; MACROPHAGE; MONOCYTE; PRIORITY JOURNAL; RNA INTERFERENCE; SIGNAL TRANSDUCTION; THP 1 CELL LINE;

EXTRACELLULAR SIGNAL-REGULATED KINASE; INTERFERON; LEUCINE-RICH REPEAT KINASE; MACROPHAGES; MITOGEN-ACTIVATED PROTEIN KINASE; SIGNAL TRANSDUCTION;

BLOTTING, WESTERN; CELLS, CULTURED; CYTOKINES; ENZYME INDUCTION; ENZYME INHIBITORS; HUMANS; IMMUNOHISTOCHEMISTRY; INTERFERON-GAMMA; MACROPHAGES; MITOGEN-ACTIVATED PROTEIN KINASE 7; PROTEIN-SERINE-THREONINE KINASES; REAL-TIME POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION;

EID: 84902360686     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.12668     Document Type: Article

References (34)

1. Barrett J. C., Hansoul S., Nicolae D. L., et al,. (2008) Genome-wide association defines more than 30 distinct susceptibility loci for Crohn's disease. Nat. Genet. 40, 955-962.
2. Cookson M. R., (2010) The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease. Nat. Rev. Neurosci. 11, 791-797.
3. Covy J. P., and, Giasson B. I., (2009) Identification of compounds that inhibit the kinase activity of leucine-rich repeat kinase 2. Biochem. Biophys. Res. Commun. 378, 473-477.
4. Deng X., Dzamko N., Prescott A., et al,. (2011) Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2. Nat. Chem. Biol. 7, 203-205.
5. Díaz-Rodríguez E., and, Pandiella A., (2010) Multisite phosphorylation of Erk5 in mitosis. J. Cell Sci. 123, 3146-3156.
6. 935, disruption of 14-3-3 binding and altered cytoplasmic localization. Biochem. J. 430, 405-413.
7. Erazo T., Moreno A., Ruiz-Babot G., Rodríguez-Asiain A., Morrice N. A., Espadamala J., Bayascas J. R., Gõmez N., and, Lizcano J. M., (2013) Canonical and kinase activity-independent mechanisms for extracellular signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation of Hsp90 from the ERK5-Cdc37 complex. Mol. Cell. Biol. 33, 1671-1686.
8. Galter D., Westerlund M., Carmine A., Lindqvist E., Sydow O., and, Olson L., (2006) LRRK2 expression linked to dopamine-innervated areas. Ann. Neurol. 59, 714-719.
9. Gardet A., Benita Y., Li C., et al,. (2010) LRRK2 is involved in the IFN-γ response and host response to pathogens. J. Immunol. 185, 5577-5585.
10. Goh K. C., Haque S. J., and, Williams B. R., (1999) p38 MAP kinase is required for STAT1 serine phosphorylation and transcriptional activation induced by interferons. EMBO J. 18, 5601-5608.
11. Greggio E., Civiero L., Bisaglia M., and, Bubacco L., (2012) Parkinson's disease and immune system: is the culprit LRRKing in the periphery? J. Neuroinflammation 9, 94.
12. Hakimi M., Selvanantham T., Swinton E., et al,. (2011) Parkinson's disease-linked LRRK2 is expressed in circulating and tissue immune cells and upregulated following recognition of microbial structures. J. Neural. Transm. 118, 795-808.
13. Hayashi M., and, Lee J. D., (2004) Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice. J. Mol. Med. (Berl) 82, 800-808.
14. Katsoulidis E., Li Y., Yoon P., et al,. (2005) Role of the p38 mitogen-Activated protein kinase pathway in cytokine-mediated hematopoietic suppression in myelodysplastic syndromes. Cancer Res. 65, 9029-9037.
15. Liu Z., Lee J., Krummey S., Lu W., Cai H., and, Lenardo M. J., (2011) The kinase LRRK2 is a regulator of the transcription factor NFAT that modulates the severity of inflammatory bowel disease. Nat. Immunol. 12, 1063-1070.
16. Luerman G. C., Nguyen C., Samaroo H., et al,. (2013) Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN-1. J. Neurochem. 128, 561-576.
17. Moehle M. S., Webber P. J., Tse T., Sukar N., Standaert D. G., DeSilva T. M., Cowell R. M., and, West A. B., (2012) LRRK2 inhibition attenuates microglial inflammatory responses. J. Neurosci. 32, 1602-1611.
18. Morimoto H., Kondoh K., Nishimoto S., Terasawa K., and, Nishida E., (2007) Activation of a C-terminal transcriptional activation domain of ERK5 by autophosphorylation. J. Biol. Chem. 282, 35449-35456.
19. Nichols R. J., Dzamko N., Hutti J. E., Cantley L. C., Deak M., Moran J., Bamborough P., Reith A. D., and, Alessi D. R., (2009) Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease. Biochem. J. 424, 47-60.
20. Nithianandarajah-Jones G. N., Wilm B., Goldring C. E., Müller J., and, Cross M. J., (2012) ERK5: structure, regulation and function. Cell. Signal. 24, 2187-2196.
21. Paisán-Ruíz C., Jain S., Evans E. W., et al,. (2004) Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease. Neuron 44, 595-600.
22. Ramsden N., Perrin J., Ren Z., et al,. (2011) Chemoproteomics-based design of potent LRRK2-selective lead compounds that attenuate Parkinson's disease-related toxicity in human neurons. ACS Chem. Biol. 6, 1021-1028.
23. Satake W., Nakabayashi Y., Mizuta I., et al,. (2009) Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease. Nat. Genet. 41, 1303-1307.
24. Simõn-Sánchez J., Schulte C., Bras J. M., et al,. (2009) Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nat. Genet. 41, 1308-1312.
25. Sloan M., Alegre-Abarrategui J., and, Wade-Martins R., (2012) Insights into LRRK2 function and dysfunction from transgenic and knockout rodent models. Biochem. Soc. Trans. 40, 1080-1085.
26. Tatake R. J., O'Neill M. M., Kennedy C. A., et al,. (2008) Identification of pharmacological inhibitors of the MEK5/ERK5 pathway. Biochem. Biophys. Res. Commun. 377, 120-125.
27. Valledor A. F., Sánchez-Tillõ E., Arpa L., Park J. M., Caelles C., Lloberas J., and, Celada A., (2008) Selective roles of MAPKs during the macrophage response to IFN-γ. J. Immunol. 180, 4523-4529.
28. de Weerd N. A., and, Nguyen T., (2012) The interferons and their receptors-distribution and regulation. Immunol. Cell Biol. 90, 483-491.
29. Yang Q., Deng X., Lu B., Cameron M., Fearns C., Patricelli M. P., Yates J. R., 3rd, Gray N. S., and, Lee J.-D., (2010) Pharmacological inhibition of BMK1 suppresses tumor growth through promyelocytic leukemia protein. Cancer Cell 18, 258-267.
30. Yin Y., She H., Li W., Yang Q., Guo S., and, Mao Z., (2012) Modulation of neuronal survival factor MEF2 by kinases in Parkinson's disease. Front. Physiol. 3, 171.
31. Yue Z., (2012) Genetic mouse models for understanding LRRK2 biology, pathology and pre-clinical application. Parkinsonism Relat. Disord. 18 (Suppl 1), S180-S182.
32. Zhang F.-R., Huang W., Chen S.-M., et al,. (2009) Genomewide association study of leprosy. N. Engl. J. Med. 361, 2609-2618.
33. Zhang J., Deng X., Choi H. G., Alessi D. R., and, Gray N. S., (2012) Characterization of TAE684 as a potent LRRK2 kinase inhibitor. Bioorg. Med. Chem. Lett. 22, 1864-1869.
34. Zimprich A., Biskup S., Leitner P., et al,. (2004) Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron 44, 601-607.