Role of a Pineal cAMP-Operated Arylalkylamine N-Acetyltransferase/14-3-3-Binding Switch in Melatonin Synthesis

The daily rhythm in melatonin levels is controlled by cAMP through actions on the penultimate enzyme in melatonin synthesis, arylalkylamine N-acetyltransferase (AANAT; serotonin N-acetyltransferase, EC 2.3.1.87). Results presented here describe a regulatory/binding sequence in AANAT that encodes a c...

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Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 98; no. 14; pp. 8083 - 8088
Main Authors:	Ganguly, Surajit, Gastel, Jonathan A., Weller, Joan L., Schwartz, Christian, Jaffe, Howard, Namboodiri, M. A. A., Coon, Steven L., Hickman, Alison B., Rollag, Mark, Obsil, Tomas, Beauverger, Philippe, Ferry, Gilles, Boutin, Jean A., Klein, David C.
Format:	Journal Article
Language:	English
Published:	United States National Academy of Sciences 03-07-2001 National Acad Sciences The National Academy of Sciences
Subjects:	14-3-3 Proteins Animals Antiserum Arylalkylamine N-Acetyltransferase Arylamine N-Acetyltransferase - physiology Biological Sciences Cell lines CHO Cells Cricetinae Dimers Elution Enzymes Hormones Humans Melatonin - physiology Monomers Neurology Phosphorylation Physiological regulation Pineal Gland - physiology Proteins Teeth Transfection Tyrosine 3-Monooxygenase - physiology
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Summary:	The daily rhythm in melatonin levels is controlled by cAMP through actions on the penultimate enzyme in melatonin synthesis, arylalkylamine N-acetyltransferase (AANAT; serotonin N-acetyltransferase, EC 2.3.1.87). Results presented here describe a regulatory/binding sequence in AANAT that encodes a cAMP-operated binding switch through which cAMP-regulated protein kinase-catalyzed phosphorylation [RRHTLPAN → RRHpTLPAN] promotes formation of a complex with 14-3-3 proteins. Formation of this AANAT/14-3-3 complex enhances melatonin production by shielding AANAT from dephosphorylation and/or proteolysis and by decreasing the Kmfor 5-hydroxytryptamine (serotonin). Similar switches could play a role in cAMP signal transduction in other biological systems.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 S.G. and J.A.G. contributed equally to this work. Edited by Martha Vaughan, National Institutes of Health, Rockville, MD, and approved May 4, 2001 To whom reprint requests should be addressed. E-mail: klein@helix.nih.gov.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.141118798