Global ubiquitome analysis of substantia nigra in doubly-mutant human alpha-synuclein transgenic mice

doi:10.1016/j.bbr.2019.112436

. 2020 Feb 17:380:112436.

doi: 10.1016/j.bbr.2019.112436. Epub 2019 Dec 14.

Global ubiquitome analysis of substantia nigra in doubly-mutant human alpha-synuclein transgenic mice

Feng He¹, Lijun Zhang¹, Guangjian Qi¹, Qian Zhang¹, Hongwei Cai¹, Tongxia Li¹, Ming Li¹, Jie Ming², Bo Tian³, Pei Zhang⁴

Affiliations

¹ Department of Neurobiology, Tongji Medical School, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China.
² Department of Breast and Thyroid Surgery, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei Province, 430030, PR China.
³ Department of Neurobiology, Tongji Medical School, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Key Laboratory of Neurological Diseases, Ministry of Education, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Institute for Brain Research, Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China. Electronic address: tianbo@mails.tjmu.edu.cn.
⁴ Department of Neurobiology, Tongji Medical School, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Key Laboratory of Neurological Diseases, Ministry of Education, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Institute for Brain Research, Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Suizhou Hospital, Hubei University of Medicine, Suizhou, Hubei Province, 442000, PR China. Electronic address: zhangpei@hust.edu.cn.

PMID: 31846630
DOI: 10.1016/j.bbr.2019.112436

Global ubiquitome analysis of substantia nigra in doubly-mutant human alpha-synuclein transgenic mice

Feng He et al. Behav Brain Res. 2020.

. 2020 Feb 17:380:112436.

doi: 10.1016/j.bbr.2019.112436. Epub 2019 Dec 14.

Authors

Feng He¹, Lijun Zhang¹, Guangjian Qi¹, Qian Zhang¹, Hongwei Cai¹, Tongxia Li¹, Ming Li¹, Jie Ming², Bo Tian³, Pei Zhang⁴

Affiliations

¹ Department of Neurobiology, Tongji Medical School, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China.
² Department of Breast and Thyroid Surgery, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei Province, 430030, PR China.
³ Department of Neurobiology, Tongji Medical School, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Key Laboratory of Neurological Diseases, Ministry of Education, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Institute for Brain Research, Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China. Electronic address: tianbo@mails.tjmu.edu.cn.
⁴ Department of Neurobiology, Tongji Medical School, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Key Laboratory of Neurological Diseases, Ministry of Education, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Institute for Brain Research, Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei Province, 430030, PR China; Suizhou Hospital, Hubei University of Medicine, Suizhou, Hubei Province, 442000, PR China. Electronic address: zhangpei@hust.edu.cn.

PMID: 31846630
DOI: 10.1016/j.bbr.2019.112436

Abstract

Progression through neuronal loss of substantia nigra pars compacta (SNpc) with Parkinson's disease depends on various protein post-translational modifications mainly comprising ubiquitination. Although many ubiquitination sites have been identified through site-specific methods, systematic quantitative proteomic analysis of pre-symptomatic Parkinson's disease remains unexplored. Using quantitative proteomics, we have globally profiled ubiquitination in SNpc tissue of a Parkinson's disease transgenic mouse model (A30P*A53 T α-synuclein, hm²α-SYN-39 mouse strain) at pre-symptomatic stage; Our datasets of 3971 ubiquitination sites in 1595 proteins provide valuable insight into pre-symptomatic Parkinson's disease. Subsequent bioinformatics analysis, including gene ontology analysis, KEGG pathway annotation, functional cluster analysis, and motif analysis were performed to annotate quantifiable targets of ubiquitination sites. Therefore, this elucidation of the dysregulation of ubiquitination has implications for understanding the pathophysiological mechanism of dopaminergic neuron degeneration and for developing novel therapeutics for Parkinson's disease.

Keywords: Alpha-synuclein; Parkinson’s disease; Quantitative proteomics; Ubiquitination.

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Global ubiquitome analysis of substantia nigra in doubly-mutant human alpha-synuclein transgenic mice

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Global ubiquitome analysis of substantia nigra in doubly-mutant human alpha-synuclein transgenic mice

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