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

被引：162

作者：

Ganguly, S

Gastel, JA

Weller, JL

Schwartz, C

Jaffe, H

Namboodiri, MAA

Coon, SL

Hickman, AB

Rollag, M

Obsil, T

Beauverger, P

Ferry, G

Boutin, JA

Klein, DC ^{[1
]}

机构：

[1] NICHHD, Dev Neurobiol Lab, Sect Neuroendocrinol, NIH, Bethesda, MD 20892 USA

[2] NINDS, Prot Sequencing Facil, NIH, Bethesda, MD 20892 USA

[3] Uniformed Serv Univ Hlth Sci, Dept Anat Physiol & Genet, Circadian Res Ctr, Bethesda, MD 20814 USA

[4] NIDDKD, Mol Biol Lab, NIH, Bethesda, MD 20892 USA

[5] Inst Rech Servier, F-78290 Croissy Sur Seine, France

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2001年 / 98卷 / 14期

关键词：

D O I：

10.1073/pnas.141118798

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The daily rhythm in melatonin levels is controlled by cAMP through actions on the penultimate enzyme in melatonin synthesis, arylalkylamine IV-acetyltransferase (AANAT; serotonin IV-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 K-m for 5-hydroxytryptamine (serotonin). Similar switches could play a role in cAMP signal transduction in other biological systems.

引用

页码：8083 / 8088

页数：6

共 24 条

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