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

Research output: Chapter in Book/Report/Conference proceedingChapter

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Title of host publicationAdvances in Pharmacology
PublisherAcademic Press Inc.
Pages3-11
Number of pages9
DOIs
Publication statusPublished - 01-01-2013

Publication series

NameAdvances in Pharmacology
Volume68
ISSN (Print)1054-3589
ISSN (Electronic)1557-8925

Fingerprint

Tyrosine 3-Monooxygenase
Digestion
Phosphorylation
Enzymes
Proteasome Endopeptidase Complex
Ubiquitin
Neurodegenerative Diseases
Catecholamines
Parkinson Disease
Proteins

All Science Journal Classification (ASJC) codes

  • Pharmacology

Cite this

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

Intracellular stability of tyrosine hydroxylase. Phosphorylation and proteasomal digestion of the enzyme. / Nakashima, Akira; Kaneko, Yoko S.; Kodani, Yu; Mori, Keiji; Nagasaki, Hiroshi; Nagatsu, Toshiharu; Ota, Akira.

Advances in Pharmacology. Academic Press Inc., 2013. p. 3-11 (Advances in Pharmacology; Vol. 68).

Research output: Chapter in Book/Report/Conference proceedingChapter

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AU - Nagatsu, Toshiharu

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AB - 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.

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