14‐3‐3 Proteins in Pineal Photoneuroendocrine Transduction: How Many Roles?
- 6 March 2003
- journal article
- review article
- Published by Wiley in Journal of Neuroendocrinology
- Vol. 15 (4) , 370-377
- https://doi.org/10.1046/j.1365-2826.2003.01000.x
Abstract
Recent studies suggest that a common theme links the diverse elements of pineal photoneuroendocrine transduction –regulation via binding to 14‐3‐3 proteins. The elements include photoreception, neurotransmission, signal transduction and the synthesis of melatonin from tryptophan. We review general aspects of 14‐3‐3 proteins and their biological function as binding partners, and also focus on their roles in pineal photoneuroendocrine transduction.Keywords
This publication has 49 references indexed in Scilit:
- Control of melatonin synthesis in the mammalian pineal gland: the critical role of serotonin acetylationCell and tissue research, 2002
- Brain 14‐3‐3 protein is an activator protein that activates tryptophan 5‐monooxygenase and tyrosine 3‐monooxygenase in the presence of Ca2+,calmodulin‐dependent protein kinase IIPublished by Wiley ,2001
- Interaction of 14-3-3 with a Nonphosphorylated Protein Ligand, Exoenzyme S ofPseudomonas aeruginosaBiochemistry, 1999
- Stimulation of catecholamine secretion from adrenal chromaffin cells by 14‐3‐3 proteins is due to reorganisation of the cortical actin networkFEBS Letters, 1995
- Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosisNeuron, 1995
- Demonstration of the Phosphorylation-Dependent Interaction of Tryptophan Hydroxylase with the 14-3-3 ProteinBiochemical and Biophysical Research Communications, 1993
- Activation of protein kinase C by the 14‐3‐3 proteins homologous with Exol protein that stimulates calcium‐dependent exocytosisFEBS Letters, 1992
- A major role for protein kinase C in calcium‐activated exocytosis in permeabilised adrenal chromaffin cellsFEBS Letters, 1988
- Phosphorylation of Purified Rat Striatal Tyrosine Hydroxylase by Ca2+/Calmodulin‐Dependent Protein Kinase II: Effect of an Activator ProteinJournal of Neurochemistry, 1987
- Activation of tryptophan 5-monooxygenase by calcium-dependent regulator proteinBiochemical and Biophysical Research Communications, 1979