Evidence map›Paper›PMID 20600597›Full record

ReviewNeuroscience letters2010

Analysis and functional implications of phosphorylation of neuronal voltage-gated potassium channels.

Oscar Cerda, James S Trimmer

Abstract readReview
In one paragraph

Review in Neuroscience letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Increased KCells · 2022
    Article
  5. Glycogen Synthase Kinase 3: Ion Channels, Plasticity, and Diseases.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Chronic mild stress alters synaptic plasticity in the nucleus accumbens through GSK3β-dependent modulation of Kv4.2 channels.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. Molecular determinants of beta-adrenergic signaling to voltage-gated KMicrocirculation (New York, N.Y. : 1994) · 2018
    Review
  11. Phosphorylation of the Cav3.2 T-type calcium channel directly regulates its gating properties.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Leptin modulates the intrinsic excitability of AgRP/NPY neurons in the arcuate nucleus of the hypothalamus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    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

2 authors.

Oscar CerdaDepartment of Neurobiology, Physiology and Behavior, University of California, Davis, CA 95616-8519, United States.
James S Trimmer

Funding

Determinants of Dendritic Potassium Channel LocalizationR01NS042225 · NINDS · UNIVERSITY OF CALIFORNIA DAVIS · PI TRIMMER, JAMES S · 2001 to 2014
$6.3M
K+ CHANNEL ALPHA AND BETA SUBUNIT INTERACTIONSR37NS034383 · NINDS · UNIVERSITY OF CALIFORNIA DAVIS · PI TRIMMER, JAMES S · 2000 to 2006
$2.6M
K+ Channel Alpha & Beta Subunit InteractionR01NS034383 · NINDS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI TRIMMER, JAMES S · 1995 to 2012
$1.7M
Phosphorylation as a Determinant of BK Channel Expression and LocalizationR21NS064957 · NINDS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI TRIMMER, JAMES S · 2009 to 2010
$421k
NINDS NIH HHS NS34383NINDS NIH HHS NS42225NINDS NIH HHS R01 NS034383NINDS NIH HHS R01 NS042225NINDS NIH HHS R21 NS064957NINDS NIH HHS R37 NS034383
6 · The paper itself

Abstract

Phosphorylation is the most common and abundant post-translational modification to eukaryotic proteins, regulating a plethora of dynamic cellular processes. Here, we review and discuss recent advances in our knowledge of the breadth and importance of reversible phosphorylation in regulating the expression, localization and function of mammalian neuronal voltage-gated potassium (Kv) channels, key regulators of neuronal function. We highlight the role of modern mass spectrometric techniques and phosphospecific antibodies in revealing the extent and nature of phosphorylation at specific sites in Kv channels. We also emphasize the role of reversible phosphorylation in dynamically regulating diverse aspects of Kv channel biology. Finally, we discuss as important future directions the determination of the mechanistic basis for how altering phosphorylation state affects Kv channel expression, localization and function, the nature of macromolecular signaling complexes containing Kv channels and enzymes regulating their phosphorylation state, and the specific role of Kv channel phosphorylation in regulating neuronal function during physiological and pathophysiological events.

Indexed as

AnimalsAntibodiesHumansImmunoassayMultiprotein ComplexesNeuronsPhosphoproteinsPhosphorylationPotassium Channels, Voltage-GatedProteomicsSignal TransductionTandem Mass SpectrometryAntibodiesMultiprotein ComplexesPhosphoproteinsPotassium Channels, Voltage-Gated

Identifiers

PMID20600597
PMCPMC3365921

What OpenQuestion holds

Textmetadata
LicenceTDM
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.