2013年
Intracellular stability of tyrosine hydroxylase. Phosphorylation and proteasomal digestion of the enzyme.
Advances in Pharmacology
- ,
- ,
- ,
- ,
- ,
- ,
- 巻
- 68
- 号
- 開始ページ
- 3
- 終了ページ
- 11
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/B978-0-12-411512-5.00001-4
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. © 2013 Elsevier Inc.
- リンク情報
- ID情報
-
- DOI : 10.1016/B978-0-12-411512-5.00001-4
- ISSN : 1054-3589
- ISSN : 1557-8925
- PubMed ID : 24054137
- SCOPUS ID : 84884325273