Evidence map›Paper›PMID 23307288›Full record

ArticleMolecules and cells2013

Ubiquilin 1 interacts with Orai1 to regulate calcium mobilization.

Jeong-Eun Lee, In-Sook Jeon, Na-Eun Han, Hye-Jin Song, Eung-Gook Kim, Jae-Woon Choi, Ki-Duk Song, Hak-Kyo Lee, Joong-Kook Choi

Open access · bronzeAbstract read
In one paragraph

Article in Molecules and cells, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Orai1 acts as a novel CaExperimental & molecular medicine · 2026
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  3. Store-operated calcium entry-based targets for novel cancer therapeutic development.The Journal of pharmacology and experimental therapeutics · 2025
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  4. Neuronal Store-Operated Calcium Channels.Molecular neurobiology · 2023
    Review
  5. Article
  6. PKC-β modulates CaGenes & genomics · 2022
    Article
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  8. Review
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  12. Article
  13. Article
  14. Review
  15. Article
  16. CD47 signaling pathways controlling cellular differentiation and responses to stress.Critical reviews in biochemistry and molecular biology · 2015
    Review
  17. 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

9 authors at 2 institutions in 1 country.

Jeong-Eun LeeDivision of Biochemistry, Chungbuk National University, Cheongju, 361-763, Korea.
In-Sook Jeon
Na-Eun Han
Hye-Jin Song
Eung-Gook Kim
Jae-Woon Choi
Ki-Duk Song
Hak-Kyo Lee
Joong-Kook Choi
Chungbuk National University · KRHankyong National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Store-operated calcium entry (SOCE) channels composed of Stim and Orai proteins play a critical role in diverse biological processes. Upon endoplasmic reticulum (ER)-mediated calcium (Ca(2+)) depletion, Stim proteins oligomerize with Orai to initiate Ca(2+) influx across the plasma membrane. The ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains of ubiquilin 1 are involved in the degradation of presenilin and polyglutamine proteins. Through screening of Orai1 interaction partner(s) that might have an effect on SOCE, ubiquilin 1 was identified as a target of Orai1. However, the UBL and UBA domains of ubiquilin 1 were dispensable for this interaction. Additionally, ubiquilin 1 and Orai1 colocalized in the cytosolic compartment. Ubiquilin 1 increased the ubiquitination of Orai1, resulting in the formation of a high-molecular-weight form. MG132, a proteasome inhibitor, failed to block the degradation of Orai1, whereas bafilomycin A, a lysosome inhibitor, prevented Orai1 degradation. Confocal microscopy studies demonstrated that a fraction of Orai1 colocalized with ubiquilin 1 and the autophagosomal marker LC3. Because Orai1 is a constituent of SOCE, we determined the effect of ubiquilin 1 on Orai1-mediated Ca(2+) influx. As we expected, intracellular Ca(2+) mobilization, a process normally potentiated by Orai1, was downregulated by ubiquilin 1. Taken together, these findings suggest that ubiquilin 1 downregulates intracellular Ca(2+) mobilization and its downstream signaling by promoting the ubiquitination and lysosomal degradation of Orai1.

Indexed as

Calcium SignalingAdaptor Proteins, Signal TransducingAutophagy-Related ProteinsBlotting, WesternCalciumCalcium ChannelsCarrier ProteinsCell Cycle ProteinsCysteine Proteinase InhibitorsCytosolEnzyme InhibitorsHEK293 CellsHeLa CellsHumansImmunoprecipitationLeupeptinsAdaptor Proteins, Signal TransducingAutophagy-Related Proteinsbafilomycin Abenzyloxycarbonylleucyl-leucyl-leucine aldehydeCalciumCalcium ChannelsCarrier ProteinsCell Cycle ProteinsCysteine Proteinase InhibitorsEnzyme InhibitorsLeupeptinsMacrolidesMembrane ProteinsNeoplasm ProteinsORAI1 ProteinORAI1 protein, humanProteasome Endopeptidase ComplexProton-Translocating ATPasesSTIM1 protein, humanStromal Interaction Molecule 1UBQLN1 protein, human

Identifiers

PMID23307288
PMCPMC3887852
OpenAlexW2139259373

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.