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Division of Basic Geriatrics

Subject Research Institute for Neurological Diseases and Geriatrics
Division of Basic Geriatrics
staff
Lecturer:Yoshihisa Watanabe
Assistant Professor :Atsushi Tsujimura
Research Contents

 Aging is a major risk factor for several common neurodegenerative diseases. Our research interests are focused on the understanding of the molecular mechanisms which lead to neurodegenerative diseases such as Parkinson's disease (PD) and Amyotrophic lateral sclerosis (ALS). The pathogenesis of these diseases involves the accumulation of toxic protein aggregates including α-synuclein, TDP-43, and SOD1. We investigate the clearance and seeding mechanisms of toxic α-synuclein species. Main ongoing research themes are listed below.

 
  1. Molecular mechanism of autophagic clearance of α-synuclein aggregates
  2. Seeding mechanism of α-synuclein fibrils and lysosomal proteolytic system
  3. ALS-associated protein p62/SQSTM1 and proteostasis including autophagy and inclusion formation

 

Achievements
Watanabe Y.,Tsujimura A.,Taguchi K.,Tanaka M.(2016)HSF1 stress
response pathway regulates autophagy receptor SQSTM/p62-associated
proteostasis.Autophagy,in press.
Taguchi K, Watanabe Y, Tsujimura A, Tanaka M. (2016) Brain region-dependent differential expression of alpha-synuclein. J Comp Neurol 524: 1236-1258.
 
Tsujimura A, Taguchi K, Watanabe Y, Tatebe H, Tokuda T, Mizuno T, Tanaka M. (2015) Lysosomal enzyme cathepsin B enhances the aggregate forming activity of exogenous α-synuclein fibrils. Neurobiol Dis 73: 244-253.
 
Taguchi K, Watanabe Y, Tsujimura A, Tatebe H, Miyata S, Tokuda T, Mizuno T, Tanaka M. (2014) Differential expression of alpha-synuclein in hippocampal neurons. PLoS ONE 9: e89327.
 
Watanabe, Y., Tsujimura, A., Taguchi, K., Tanaka, M. (2013) α-Synuclein metabolism and aggregation in the pathogenesis of Parkinson’s disease. In: α-Synuclein: Functional Mechanisms, Structure and Role in Parkinson’s Disease. Nova Science Publishers Inc, New York. Sep. 27, 29-50.
 
Watanabe Y, Tatebe H, Taguchi K, Endo Y, Tokuda T, Mizuno T, Nakagawa M, Tanaka M. p62/SQSTM1-dependent autophagy of Lewy body-like α-synuclein inclusions. PLoS One 7: e52868, 2012.
 
Watanabe Y, Tanaka M. p62/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate. J Cell Sci 124: 2692-2701, 2011.
 
Watanabe, Y. and Tanaka, M. (2011) Physiological functions and pathology of neurosin/kallikrein 6 in the central nervous system. In: Chiba, I. and Kamio, T. editors. Serine Proteases: Mechanism, Structure and Evolution. Nova Science Publishers Inc, New York. Sep. 30, 129-137.
Contact tel 81-75-251-5848
fax 81-75-251-5797
mailto:y-watana@koto.kpu-m.ac.jp
HP

http://www.f.kpu-m.ac.jp/k/cellbio/front_E.html


602-8566 Kyoto-shi, Kamigyo-ku Kajii-cho,
Kawaramachi-Hirokoji, JAPAN

Contact
TEL:075-251-5111
FAX:075-251-7093