Evidence map›Paper›PMID 18003854›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007

Phosphorylation of the Ca2+-binding protein CaBP4 by protein kinase C zeta in photoreceptors.

Amy Lee, Amber Jimenez, Guiying Cui, Françoise Haeseleer

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Regulation of Presynaptic Calcium Channels.Advances in neurobiology · 2023
    Article
  2. Article
  3. Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019
    Review
  4. Heteromeric MTExperimental eye research · 2018
    Article
  5. Sense and specificity in neuronal calcium signalling.Biochimica et biophysica acta · 2015
    Review
  6. Article
  7. Distinct expression and localization of diacylglycerol kinase isozymes in rat retina.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2013
    Article
  8. Protein phosphatase 2A dephosphorylates CaBP4 and regulates CaBP4 function.Investigative ophthalmology & visual science · 2013
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. PPEF/PP7 protein Ser/Thr phosphatases.Cellular and molecular life sciences : CMLS · 2009
    Review
  17. Article
  18. Characterization of Ca2+-binding protein 5 knockout mouse retina.Investigative ophthalmology & visual science · 2008
    Article
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

4 authors at 2 institutions in 1 country.

Amy LeeDepartment of Pharmacology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Amber Jimenez
Guiying Cui
Françoise Haeseleer
University of Washington · USEmory University · US

Funding

Regulation of neuronal calcium channels by CaBP1R01NS044922 · NINDS · EMORY UNIVERSITY · PI LEE, AMY · 2003 to 2007
$1.6M
CaBP4, a Photoreceptor Specific Calcium-Binding ProteinR03EY014561 · NEI · UNIVERSITY OF WASHINGTON · PI HAESELEER, FRANCOISE J · 2003 to 2005
$455k
NEI NIH HHS EY014561NEI NIH HHS R03 EY014561NINDS NIH HHS NS044922NINDS NIH HHS R01 NS044922
6 · The paper itself

Abstract

CaBP4 is a calmodulin-like neuronal calcium-binding protein that is crucial for the development and/or maintenance of the cone and rod photoreceptor synapse. Previously, we showed that CaBP4 directly regulates Ca(v)1 L-type Ca2+ channels, which are essential for normal photoreceptor synaptic transmission. Here, we show that the function of CaBP4 is regulated by phosphorylation. CaBP4 is phosphorylated by protein kinase C zeta (PKCzeta) at serine 37 both in vitro and in the retina and colocalizes with PKCzeta in photoreceptors. CaBP4 phosphorylation is greater in light-adapted than dark-adapted mouse retinas. In electrophysiological recordings of cells transfected with Ca(v)1.3 and CaBP4, mutation of the serine 37 to alanine abolished the effect of CaBP4 in prolonging the Ca2+ current through Ca(v)1.3 channel, whereas inactivating mutations in the CaBP4 Ca2+-binding sites strengthened Ca(v)1.3 modulation. These findings demonstrate how light-stimulated changes in CaBP4 phosphorylation and Ca2+ binding may regulate presynaptic Ca2+ signals in photoreceptors.

Indexed as

Adaptation, OcularAmino Acid SubstitutionAnimalsBinding SitesCalciumCalcium-Binding ProteinsCalcium Channels, L-TypeCalcium SignalingMembrane PotentialsMiceMice, Inbred C57BLMice, KnockoutNerve Tissue ProteinsPhosphorylationPhotic StimulationPhotoreceptor Cells, VertebrateCabp4 protein, mouseCacna1d protein, mouseCalciumCalcium-Binding ProteinsCalcium Channels, L-TypeNerve Tissue ProteinsProtein Kinase Cprotein kinase C zeta II, mouseSerine

Identifiers

PMID18003854
PMCPMC2703458
OpenAlexW2009974340

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.