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Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis.

Authors :
Ganguly S
Gastel JA
Weller JL
Schwartz C
Jaffe H
Namboodiri MA
Coon SL
Hickman AB
Rollag M
Obsil T
Beauverger P
Ferry G
Boutin JA
Klein DC
Source :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2001 Jul 03; Vol. 98 (14), pp. 8083-8. Date of Electronic Publication: 2001 Jun 26.
Publication Year :
2001

Abstract

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 ). 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 K(m) for 5-hydroxytryptamine (serotonin). Similar switches could play a role in cAMP signal transduction in other biological systems.

Details

Language :
English
ISSN :
0027-8424
Volume :
98
Issue :
14
Database :
MEDLINE
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Publication Type :
Academic Journal
Accession number :
11427721
Full Text :
https://doi.org/10.1073/pnas.141118798