Evidence map›Paper›PMID 21689744›Full record

ArticleCellular signalling2011

CaMK IV phosphorylates prohibitin 2 and regulates prohibitin 2-mediated repression of MEF2 transcription.

Luguo Sun, Xia Cao, Bin Liu, Honglan Huang, Xu Wang, Liyan Sui, Weimin Yin, Kewei Ma

Open access · bronzeAbstract read
In one paragraph

Article in Cellular signalling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

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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.

Luguo SunInstitute of Genetics and Cytology, Northeast Normal University, Changchun, China.
Xia Cao
Bin Liu
Honglan Huang
Xu Wang
Liyan Sui
Weimin Yin
Kewei Ma
First Hospital of Jilin University · CNJilin University · CNFirst Bethune Hospital of Jilin University · CNNortheast Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prohibitin 2 (PHB2) is an evolutionarily conserved and ubiquitously expressed multifunctional protein which is present in various cellular compartments including the nucleus. However, mechanisms underlying various functions of PHB2 are not fully explored yet. Previously we showed that PHB2 interacts with Akt and inhibits muscle differentiation by repressing the transcriptional activity of both MyoD and MEF2. Here we show that Calcium/Calmodulin-dependent kinase IV (CaMK IV) specifically binds to the C terminus of PHB2 and phosphorylates PHB2 at serine 91. Ectopic expression of CaMK IV and PHB2 in C2C12 cells results effectively in decreased PHB2-mediated repression of MEF2-dependent gene expression. Conversely, PHB2 mutant (S91A) resistant to CaMK IV phosphorylation has less effective in relieving the inhibition of MEF2 transcription by PHB2. Our findings suggest that CaMK IV interacts with and regulates PHB2 through phosphorylation, which could be one of the mechanisms underlying the CaMK-mediated activation of MEF2.

Indexed as

Transcription, GeneticAnimalsBlotting, WesternCalcium-Calmodulin-Dependent Protein Kinase Type 4Cell LineGene Expression RegulationImmunoprecipitationMiceMyogenic Regulatory FactorsPhosphorylationProhibitinsRecombinant Fusion ProteinsRepressor ProteinsSubstrate SpecificityTranscriptional ActivationTranscription FactorsCalcium-Calmodulin-Dependent Protein Kinase Type 4Myogenic Regulatory FactorsPhb2 protein, mouseProhibitinsRecombinant Fusion ProteinsRepressor ProteinsTranscription Factors

Identifiers

PMID21689744
PMCPMC7127762
OpenAlexW2019351056

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.