Intracellular stability of tyrosine hydroxylase. Phosphorylation and proteasomal digestion of the enzyme.

Akira Nakashima, Yoko S. Kaneko, Yu Kodani, Keiji Mori, Hiroshi Nagasaki, Toshiharu Nagatsu, Akira Ota

研究成果: Chapter

12 引用 (Scopus)

抜粋

Tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of catecholamines, is a key protein involved in the pathogenesis of neurodegenerative diseases such as Parkinson's disease. Elucidation of the mechanisms regulating the synthesis, degradation, and activity of TH should be a first target in order to understand the role of this enzyme in pathogenesis. Recently, several reports suggest that the ubiquitin-proteasome pathway is a prerequisite for the degradation of TH and that the N-terminal part of TH plays a critical role in the degradation. In this report, we propose the mechanism by which the N-terminal part of TH regulates the degradation of this enzyme. Moreover, we integrate our findings with recent progress in other areas of TH regulation.

元の言語English
ホスト出版物のタイトルAdvances in Pharmacology
出版者Academic Press Inc.
ページ3-11
ページ数9
DOI
出版物ステータスPublished - 2013

出版物シリーズ

名前Advances in Pharmacology
68
ISSN(印刷物)1054-3589
ISSN(電子版)1557-8925

All Science Journal Classification (ASJC) codes

  • Pharmacology

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    Nakashima, A., Kaneko, Y. S., Kodani, Y., Mori, K., Nagasaki, H., Nagatsu, T., & Ota, A. (2013). Intracellular stability of tyrosine hydroxylase. Phosphorylation and proteasomal digestion of the enzyme.Advances in Pharmacology (pp. 3-11). (Advances in Pharmacology; 巻数 68). Academic Press Inc.. https://doi.org/10.1016/B978-0-12-411512-5.00001-4