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

Biochem Soc Trans. 2002 Aug;30(4):365-73. doi: 10.1042/bst0300365.

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.

Publication types

  • Review

MeSH terms

  • 14-3-3 Proteins
  • Animals
  • Arylamine N-Acetyltransferase / chemistry
  • Arylamine N-Acetyltransferase / metabolism
  • Binding Sites
  • Circadian Rhythm / physiology*
  • Light
  • Melatonin / physiology*
  • Models, Molecular
  • Neurosecretory Systems / physiology*
  • Protein Conformation
  • Signal Transduction / physiology*
  • Tyrosine 3-Monooxygenase / chemistry
  • Tyrosine 3-Monooxygenase / physiology*

Substances

  • 14-3-3 Proteins
  • Tyrosine 3-Monooxygenase
  • Arylamine N-Acetyltransferase
  • Melatonin