Dopamine or biopterin deficiency potentiates phosphorylation at 40 Ser and ubiquitination of tyrosine hydroxylase to be degraded by the ubiquitin proteasome system-Reference-Cited by-同舟云学术

Dopamine or biopterin deficiency potentiates phosphorylation at 40 Ser and ubiquitination of tyrosine hydroxylase to be degraded by the ubiquitin proteasome system

Published:2015-09 Issue:1 Volume:465 Page:53-58
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Kawahata Ichiro,Ohtaku Shiori,Tomioka Yoshihisa,Ichinose Hiroshi^ORCID,Yamakuni Tohru

Funder

JSPS KAKENHI

the Ministry of Education, Culture, Sports, Science, and Technology of Japan

Ministry of Health, Labour and Welfare of Japan

Uehara Memorial Foundation

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference30 articles.

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3. Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy. Effect of iron/catecholamine binding and phosphorylation;Martinez;J. Biol. Chem.,1996

4. Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding;McCulloch;Arch. Biochem. Biophys.,1999

5. Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: evidence for a novel regulatory mechanism;Ramsey;Biochemistry,1998

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