| Literature DB >> 11427721 |
S Ganguly1, J A Gastel, J L Weller, C Schwartz, H Jaffe, M A Namboodiri, S L Coon, A B Hickman, M Rollag, T Obsil, P Beauverger, G Ferry, J A Boutin, D C Klein.
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.Entities:
Mesh：
Substances：
Year: 2001 PMID： 11427721 PMCID： PMC35471 DOI： 10.1073/pnas.141118798
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205