Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis.
Proc Natl Acad Sci U S A
; 98(14): 8083-8, 2001 Jul 03.
Article
in En
| MEDLINE
| ID: mdl-11427721
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Pineal Gland
/
Arylamine N-Acetyltransferase
/
Tyrosine 3-Monooxygenase
/
Melatonin
Limits:
Animals
/
Humans
Language:
En
Journal:
Proc Natl Acad Sci U S A
Year:
2001
Document type:
Article
Affiliation country:
Estados Unidos