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PMID: 12196096 Published · ppublish English Journal Article Review

14-3-3 Proteins and photoneuroendocrine transduction: role in controlling the daily rhythm in melatonin.

Biochemical Society transactions ·Vol. 30 ·No. 4 ·2002-08-00 ·Pages 365-73

Klein DC, Ganguly S, Coon S, Weller JL, Obsil T, Hickman A, Dyda F

Abstract

This paper describes the role 14-3-3 proteins play in vertebrate photoneuroendocrine transduction. 14-3-3 proteins form a complex with arylalkylamine N-acetyltransferase (AANAT), the enzyme which turns melatonin production on during the day and off at night. Complex formation is triggered at night by cAMP-dependent phosphorylation of the enzyme, and results in activation and protection against proteolysis. This enhances melatonin production >10-fold. Light exposure results in dephosphorylation of the enzyme and disassociation from 14-3-3, leading to destruction and a rapid drop in melatonin production and release and circulating levels.

MeSH Terms
14-3-3 Proteins Animals Arylamine N-Acetyltransferase/chemistry,metabolism Binding Sites Circadian Rhythm/physiology Light Melatonin/physiology Models, Molecular Neurosecretory Systems/physiology Protein Conformation Signal Transduction/physiology Tyrosine 3-Monooxygenase/chemistry,physiology
Chemicals
14-3-3 Proteins Tyrosine 3-Monooxygenase Arylamine N-Acetyltransferase Melatonin
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Klein D C
Section on Neuroendocrinology, Laboratory of Developmental Neurobiology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-4480, USA. klein@helix.nih.gov
Ganguly S
Coon S
Weller J L
Obsil T
Hickman A
Dyda F
Article Info
Journal
Biochemical Society transactions
Abbr.
Biochem Soc Trans
ISSN
0300-5127
Published
2002-08-00
Pages
365-73
Language
English
Region
England
NLM ID
7506897
Subset
IM
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