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- Title
Photic Regulation of Arylalkylamine N-Acetyltransferase Binding to 14-3-3 Proteins in Retinal Photoreceptor Cells.
- Authors
Pozdeyev, Nikita; Taylor, Carla; Haque, Rashidul; Chaurasia, Shyam S.; Visser, Amy; Thazyeen, Aamera; Yuhong Du; Haian Fu; Weller, Joan; Klein, David C.; Iuvone, P. Michael
- Abstract
14-3-3 proteins are a ubiquitous, highly conserved family of chaperone proteins involved in signal transduction, regulation of cell cycle, intracellular trafficking/targeting, cytoskeletal structure, and transcription. Although 14-3-3 proteins are among the most abundant proteins in the CNS, very little is known about their functional roles in the vertebrate retina. In the present study, we demonstrated that photoreceptors express 14-3-3 protein(s) and identified a 14-3-3 binding partner in photoreceptor cells, the melatonin-synthesizing enzyme arylalkylamine N-acetyltransferase (AANAT). Importantly, our data demonstrate that the binding of 14-3-3 to AANAT is regulated by light, with dramatic functional consequences. During the night in darkness, retinal AANAT is phosphorylated and forms a complex with 14-3-3 proteins with an apparent molecular weight of ~90 kDa. Phosphorylation of AANAT facilitates the binding of enzymeto 14-3-3 proteins.Withinthe complex, AANATis catalytically activated and protectedfrom dephosphorylation and degradation. Light disrupts the AANAT/14-3-3 complex, leading to catalytic inactivation, dephosphorylation, and proteolytic degradation of the enzyme. Inthe presence ofthe proteasome inhibitor, lactacystin, light results inthe formation of a high molecular weight complex (>150 kDa), whichmay represent anintermediateinthe AANAT degradation process. Thesefindings provide newinsightintothe roles of 14-3-3 proteins in photoreceptor cells and to the mechanisms controlling melatonin synthesis in the vertebrate retina.
- Publication
Journal of Neuroscience, 2006, Vol 26, Issue 36, p9153
- ISSN
0270-6474
- Publication type
Article
- DOI
10.1523/JNEUROSCI.1384-06.2006