Evidence map›Paper›PMID 21504899›Full record

ArticleThe Journal of biological chemistry2011

Phosphorylation of G protein-coupled receptor kinase 1 (GRK1) is regulated by light but independent of phototransduction in rod photoreceptors.

Shoji Osawa, Rebecca Jo, Yubin Xiong, Boris Reidel, Nomingerel Tserentsoodol, Vadim Y Arshavsky, P Michael Iuvone, Ellen R Weiss

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Phosphorylation at Serine 21 in G protein-coupled receptor kinase 1 (GRK1) is required for normal kinetics of dark adaption in rod but not cone photoreceptors.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  8. Article
  9. RGS Protein Regulation of Phototransduction.Progress in molecular biology and translational science · 2015
    Review
  10. Article
  11. 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

8 authors at 4 institutions in 1 country.

Shoji OsawaDepartment of Cell and Developmental Biology, University of North Carolina, Chapel Hill, North Carolina 27599-7090, USA.
Rebecca Jo
Yubin Xiong
Boris Reidel
Nomingerel Tserentsoodol
Vadim Y Arshavsky
P Michael Iuvone
Ellen R Weiss
University of North Carolina at Chapel Hill · USSmith-Kettlewell Eye Research Institute · USDuke University · USEmory University · US

Funding

VISION RESEARCHP30EY005722 · NEI · DUKE UNIVERSITY · PI Vadim Y Arshavsky · 1985 to 2026
$19.3M
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
Transducin movement and photoreceptor light adaptationR01EY010336 · NEI · UNIVERSITY OF WISCONSIN MADISON · PI ARSHAVSKY, VADIM Y · 1994 to 2012
$6.3M
NEI NIH HHS EY006360NEI NIH HHS EY072224NEI NIH HHS EY10336NEI NIH HHS EY5722NEI NIH HHS P30 EY005722NEI NIH HHS P30 EY006360NEI NIH HHS R01EY00486NEI NIH HHS R01 EY004864NEI NIH HHS R01 EY010336
6 · The paper itself

Abstract

Phosphorylation of rhodopsin by G protein-coupled receptor kinase 1 (GRK1, or rhodopsin kinase) is critical for the deactivation of the phototransduction cascade in vertebrate photoreceptors. Based on our previous studies in vitro, we predicted that Ser(21) in GRK1 would be phosphorylated by cAMP-dependent protein kinase (PKA) in vivo. Here, we report that dark-adapted, wild-type mice demonstrate significantly elevated levels of phosphorylated GRK1 compared with light-adapted animals. Based on comparatively slow half-times for phosphorylation and dephosphorylation, phosphorylation of GRK1 by PKA is likely to be involved in light and dark adaptation. In mice missing the gene for adenylyl cyclase type 1, levels of phosphorylated GRK1 were low in retinas from both dark- and light-adapted animals. These data are consistent with reports that cAMP levels are high in the dark and low in the light and also indicate that cAMP generated by adenylyl cyclase type 1 is required for phosphorylation of GRK1 on Ser(21). Surprisingly, dephosphorylation was induced by light in mice missing the rod transducin α-subunit. This result indicates that phototransduction does not play a direct role in the light-dependent dephosphorylation of GRK1.

Indexed as

LightAdenylyl CyclasesAnimalsCyclic AMPCyclic AMP-Dependent Protein KinasesDark AdaptationG-Protein-Coupled Receptor Kinase 1Light Signal TransductionMiceMice, KnockoutPhosphorylationRetinal Rod Photoreceptor CellsTransducinadenylyl cyclase 1Adenylyl CyclasesCyclic AMPCyclic AMP-Dependent Protein KinasesG-Protein-Coupled Receptor Kinase 1Grk1 protein, mouseTransducin

Identifiers

PMID21504899
PMCPMC3121460
OpenAlexW2074137152

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.