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Identification Domains of PINK1 Interacting with α-Synuclein |
FU Yue-jiao, DUAN Chun-li, GONG Pu-sheng, JIA Huan-zhen, ZHANG ian-liang, ZHAO Chun-li, LU Ling-ling, ZHAO Huan-ying, YUAN Xing-xing, YANG Hui |
Beijing Institute for Neuroscience, Capital Medical University, Beijing Center of Neural Regeneration and Repair, Key Laboratory of Neurodegenerative Diseases, Ministry of Education, Beijing 100069, China |
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Abstract Objective: To identify domains of PINK1 interacting with α-synuclein. Methods: HEK293T cells were transfected with plasmid encoding human pCMV-Myc-α-synuclein together with human 3xFlag-tagged wild type PINK1 or several deletion mutants(G309D;ΔN35; ΔC145; 156~509; Δ156~581;). After detecting the protein expression by Western blot, the functional domains of hPINK1 interacting with human α-synuclein were detected by co-immunoprecipitation. The co-localization of different domains of hPINK1 and human α-synuclein was detected by immunocytochemistry. Result: Co-IP and immunocytochemistry have proved that the PINK1 kinase domain interacted with α-synuclein. Conclusion: The kinase domain of PINK1 interacting with α-synuclein.
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Received: 26 July 2011
Published: 25 December 2011
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Cite this article:
FU Yue-jiao, DUAN Chun-li, GONG Pu-sheng, JIA Huan-zhen, ZHANG ian-liang, ZHAO Chun-li, LU Ling-ling, ZHAO Huan-ying, YUAN Xing-xing, YANG Hui. Identification Domains of PINK1 Interacting with α-Synuclein. China Biotechnology, 2011, 31(12): 10-14.
URL:
https://manu60.magtech.com.cn/biotech/ OR https://manu60.magtech.com.cn/biotech/Y2011/V31/I12/10
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[1] Forno L S. Neuropathology of Parkinson's disease.J Neuropathol Exp Neurol, 1996,55(3): 259-272.
[2] Lang A E, Lozano A M. Parkinson's disease. First of two parts. N Engl J Med, 1998, 339(1): 1044-1053.
[3] Lang A E, Lozano A M. Parkinson's disease. Second of two parts. N Engl J Med, 1998, 339(2): 1130-1143.
[4] Xie W L, Wan O W, Kenny K K, et al. New insights into the role of mitochondrial dysfunction and protein aggregation in Parkinson's disease. Biochimi Biophys Acta, 2010, 1802(11): 935-941.
[5] Spillantini M G, Crowther R A, Jakes R, et al. Alpha-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc Natl Acad Sci U S A, 1998, 95(11): 6469-6473.
[6] Spillantini M G, Schmidt M L, Lee V M, et al. Alpha-synuclein in Lewy bodies. Nature, 1997, 388(6645): 839-840.
[7] Nakamura K, Nemani V M, Wallender E K, et al. Optical reporters for the conformation of alpha-synuclein reveal a specific interaction with mitochondria. J Neurosci, 2008, 28(47) : 12305-12317.
[8] Parihar M S, Parihar A, Fujita M, et al. Mitochondrial association of alpha-synuclein causes oxidative stress. Cell Mol Life Sci, 2008, 65(7-8): 1272-1284.
[9] Martin L J, Pan Y, Price A C, et al. Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death. J Neurosci,2006,26(1):41-50.
[10] Devi L, Raghavendran V, Prabhu B M, et al. Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J Biol Chem, 2008, 283(14): 9089-9100.
[11] Valente E M, Abou-Sleiman P M, Caputo V, et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1.Science,2004,304(5674):1158-1160.
[12] Haque M E, Thomas K J,D'Souza C, et al. Cytoplasmic Pink1 activity protects neuronsfrom dopaminergic neurotoxin MPTP, Proc Natl Acad Sci U S A,2008, 105(5):1716-1721.
[13] Tan E K, PINK1 mutations and differential effects on mitochondrial function, Experimental Neurology,2010, 221(1):10-12.
[14] Kamp F, Exner N, Lutz A K. Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1. EMBO J, 2010, 29(20): 3571-3589.
[15] 范春香,崔涛,杨慧.帕金森病相关蛋白PINK1和α-突触核蛋白相互作用研究。中国生物工程杂志,2008, 28(12): 7-11. Fan C X, Cui T, Yang H. China Biotechnology, 2008, 28(12): 7-11.
[16] Mizuno Y, Hattori N, Kubo S, et al. Progress in the pathogenesis and genetics of Parkinson's disease. Phil Trans R Soc B, 2008, 363(1500): 2215-2227.
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