Evidence map›Paper›PMID 25220706›Full record

ArticleNeuroscience letters2014

Potassium channel Kv2.1 is regulated through protein phosphatase-1 in response to increases in synaptic activity.

Benjamin Siddoway, Hailong Hou, Jinnan Yang, Lu Sun, Hongtian Yang, Guo-yong Wang, Houhui Xia

Open access · greenAbstract read
In one paragraph

Article in Neuroscience letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.1field-weighted citation impact, top 47% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of PP1 interaction with I-2, neurabin, and F-actin.Molecular and cellular neurosciences · 2023
    Article
  4. Article
  5. Protein phosphatase-1 inhibitor-2 promotes PP1Frontiers in synaptic neuroscience · 2022
    Article
  6. Regulation of Synaptic Transmission and Plasticity by Protein Phosphatase 1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Review
  7. Article
  8. Protein Phosphatase-1 Inhibitor-2 Is a Novel Memory Suppressor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    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

7 authors at 2 institutions in 1 country.

Benjamin SiddowayNeuroscience Center, Louisiana State University Health Science Center, New Orleans, LA, United States. Electronic address: bsiddo@scripps.edu.
Hailong HouNeuroscience Center, Louisiana State University Health Science Center, New Orleans, LA, United States.
Jinnan YangDepartment of Structural and Cellular Biology, School of Medicine, Tulane University, New Orleans, LA, United States.
Lu SunNeuroscience Center, Louisiana State University Health Science Center, New Orleans, LA, United States.
Hongtian YangNeuroscience Center, Louisiana State University Health Science Center, New Orleans, LA, United States.
Guo-yong WangDepartment of Structural and Cellular Biology, School of Medicine, Tulane University, New Orleans, LA, United States.
Houhui XiaNeuroscience Center, Louisiana State University Health Science Center, New Orleans, LA, United States.
Louisiana State University Health Sciences Center New Orleans · USTulane University · US

Funding

Distinct role of Neurabin and Spinophilin in Synaptic Transmission and PlasticityR01NS060879 · NINDS · LSU HEALTH SCIENCES CENTER · PI XIA, HOUHUI · 2009 to 2013
$1.5M
NINDS NIH HHS NS060879NINDS NIH HHS R01 NS060879
6 · The paper itself

Abstract

The functional stability of neurons in the face of large variations in both activity and efficacy of synaptic connections suggests that neurons possess intrinsic negative feedback mechanisms to balance and tune excitability. While NMDA receptors have been established to play an important role in glutamate receptor-dependent plasticity through protein dephosphorylation, the effects of synaptic activation on intrinsic excitability are less well characterized. We show that increases in synaptic activity result in dephosphorylation of the potassium channel subunit Kv2.1. This dephosphorylation is induced through NMDA receptors and is executed through protein phosphatase-1 (PP1), an enzyme previously established to play a key role in regulating ligand gated ion channels in synaptic plasticity. Dephosphorylation of Kv2.1 by PP1 in response to synaptic activity results in substantial shifts in the inactivation curve of IK, resulting in a reduction in intrinsic excitability, facilitating negative feedback to neuronal excitability.

Indexed as

AnimalsFeedback, PhysiologicalNeuronsPhosphorylationPrimary Cell CultureProtein Phosphatase 1Rats, Sprague-DawleyReceptors, N-Methyl-D-AspartateShab Potassium ChannelsSynapsesKcnb1 protein, ratProtein Phosphatase 1Receptors, N-Methyl-D-AspartateShab Potassium ChannelsDephosphorylationKv2.1NMDA receptorPP1Synaptic activity

Identifiers

PMID25220706
PMCPMC8221410
OpenAlexW1966134699

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.