Evidence map›Paper›PMID 35254656›Full record

ArticleGenes & genomics2022

PKC-β modulates Ca

Hye-Jin Song, In-Sook Jeon, Seung Ryul Kim, Kwan Sik Park, Jae-Won Soh, Kwang Youl Lee, Jae-Cheon Shin, Hak-Kyo Lee, Joong-Kook Choi

Open access · hybridAbstract read
In one paragraph

Article in Genes & genomics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 39% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
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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

9 authors at 5 institutions in 1 country.

Hye-Jin Song *Division of Biochemistry, College of Medicine, Chungbuk National University, Ch'ongju, 28644, Korea.
In-Sook Jeon *Division of Biochemistry, College of Medicine, Chungbuk National University, Ch'ongju, 28644, Korea.
Seung Ryul KimDivision of Biochemistry, College of Medicine, Chungbuk National University, Ch'ongju, 28644, Korea.
Kwan Sik ParkDivision of Biochemistry, College of Medicine, Chungbuk National University, Ch'ongju, 28644, Korea.
Jae-Won SohBiomedical Research Center for Signal Transduction Networks, Department of Chemistry, Inha University, Incheon, 402-751, Korea.
Kwang Youl LeeCollege of Pharmacy, Chonnam National University, Gwangju, 500-757, Korea.
Jae-Cheon ShinPohang Center for Evaluation of Biomaterials, 394, Jigok-ro, Nam-gu, Pohang, Gyeongbuk, Korea.
Hak-Kyo LeeDepartment of Animal Biotechnology, Chonbuk National University, Chonju, 54896, Jeollabuk-do, Korea. breedlee@empal.com.
Joong-Kook ChoiDivision of Biochemistry, College of Medicine, Chungbuk National University, Ch'ongju, 28644, Korea. jkchoi@chungbuk.ac.kr.ORCID http://orcid.org/0000-0003-0455-971X
Chungbuk National University · KRChonnam National University · KRInha University · KRJeonbuk National University · KRPohang TechnoPark (South Korea) · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCalcium ions play a pivotal role in cell proliferation, differentiation, and migration. Under basal conditions, the calcium level is tightly regulated; however, cellular activation by growth factors increase the ion level through calcium pumps in the plasma membrane and endoplasmic reticulum for calcium signaling. Orai1 is a major calcium channel in the cell membrane of non-excitable cells, and its activity depends on the stromal interaction molecule 1 (Stim1). Several groups reported that the store-operated calcium entry (SOCE) can be modulated through phosphorylation of Stim1 by protein kinases such as extracellular signal-regulated kinase (ERK), protein kinase A (PKA), and p21-activated kinase (PAK). PKC is a protein kinase that is activated by calcium and diacylglycerol (DAG), but it remains unclear what role activated PKC plays in controlling the intracellular calcium pool.

objectivesHere, we investigated whether PKC-β controls intracellular calcium dynamics through Stim1.

methodsSeveral biochemical methods such as immune-precipitation, site directed mutagenesis, in vitro kinase assay were employed to investigate PKC interaction with and phosphorylation of Stim1. Intracellular calcium mobilization, via Stim1 mediated SOCE channel, were studied using in the presence of PKC activator or inhibitor under a confocal microscope.

resultsOur data demonstrate that PKC interacts with and phosphorylates Stim1 in vitro. phosphorylation of Stim1 at its C-terminal end appears to be important in the regulation of SOCE activity in HEK293 and HeLa cells. Additionally, transient intracellular calcium mobilization assays demonstrate that the SOCE activity was inhibited by PKC activators or activated by PKC inhibitors.

conclusionIn sum, our data suggest a repressive role of PKC in regulating calcium entry through SOCE.

Indexed as

CalciumNeoplasm ProteinsHEK293 CellsHeLa CellsHumansPhosphorylationStromal Interaction Molecule 1CalciumNeoplasm ProteinsSTIM1 protein, humanStromal Interaction Molecule 1Calcium mobilizationPKCStim1Stim1 phosphorylationStore-operated calcium entry

Identifiers

PMID35254656
PMCPMC9042968
OpenAlexW4220664346

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.