Evidence map›Paper›PMID 16957072›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006

Photic regulation of arylalkylamine N-acetyltransferase binding to 14-3-3 proteins in retinal photoreceptor cells.

Nikita Pozdeyev, Carla Taylor, Rashidul Haque, Shyam S Chaurasia, Amy Visser, Aamera Thazyeen, Yuhong Du, Haian Fu, Joan Weller, David C Klein and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.7field-weighted citation impact, top 32% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Daily Rhythm in Plasma N-acetyltryptamine.Journal of biological rhythms · 2017
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. N-acetylserotonin: neuroprotection, neurogenesis, and the sleepy brain.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2012
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Nikita PozdeyevDepartment of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Carla Taylor
Rashidul Haque
Shyam S Chaurasia
Amy Visser
Aamera Thazyeen
Yuhong Du
Haian Fu
Joan Weller
David C Klein
P Michael Iuvone
Emory University · USEunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Institutes of Health · US

Funding

P30-Core Grant for Vision Research Core CP30EY006360 · NEI · EMORY UNIVERSITY · PI BOATRIGHT, JEFFREY H · 1986 to 2025
$15.3M
Neuromodulators and Circadian Clocks: Roles in Retinal Function and DysfunctionR01EY004864 · NEI · EMORY UNIVERSITY · PI IUVONE, P MICHAEL · 1985 to 2018
$7.0M
Pineal Regulation: Control of arylalkylamine N-acetyltransferaseZ01HD008836 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI KLEIN, DAVID · 2007 to 2008
$2.0M
NEI NIH HHS P30 EY006360NEI NIH HHS P30 EY06360NEI NIH HHS R01 EY004864NEI NIH HHS R01 EY04864
6 · The paper itself

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 approximately 90 kDa. Phosphorylation of AANAT facilitates the binding of enzyme to 14-3-3 proteins. Within the complex, AANAT is catalytically activated and protected from dephosphorylation and degradation. Light disrupts the AANAT/14-3-3 complex, leading to catalytic inactivation, dephosphorylation, and proteolytic degradation of the enzyme. In the presence of the proteasome inhibitor, lactacystin, light results in the formation of a high molecular weight complex (>150 kDa), which may represent an intermediate in the AANAT degradation process. These findings provide new insight into the roles of 14-3-3 proteins in photoreceptor cells and to the mechanisms controlling melatonin synthesis in the vertebrate retina.

Indexed as

14-3-3 ProteinsAnimalsArylalkylamine N-AcetyltransferaseCells, CulturedChickensEnzyme ActivationLightMaleMelatoninPhosphorylationPhotic StimulationPhotoreceptor Cells, VertebrateProtein BindingSignal Transduction14-3-3 ProteinsArylalkylamine N-AcetyltransferaseMelatonin

Identifiers

PMID16957072
PMCPMC6674502
OpenAlexW2119269751

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.