Evidence map›Paper›PMID 10851021›Full record

ArticleThe Journal of cell biology2000

Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b.

H L Roderick, J D Lechleiter, P Camacho

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

95 citing papers in PubMed, 235 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. International journal of molecular sciences · 2026
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  9. Article
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  11. Review
  12. Arc ubiquitination regulates endoplasmic reticulum-mediated CaFrontiers in cellular neuroscience · 2023
    Article
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  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
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35 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

H L RoderickDepartment of Physiology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229-3900, USA.
J D Lechleiter
P Camacho
The University of Texas Health Science Center at San Antonio · US

Funding

LUMINAL CONTROL OF CALCIUM RELEASE BY CALRETICULINR01GM055372 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI CAMACHO, PATRICIA · 1997 to 2005
$1.6M
NIGMS NIH HHS R01 GM055372NIGMS NIH HHS R01 GM55372
6 · The paper itself

Abstract

Calreticulin (CRT) and calnexin (CLNX) are lectin chaperones that participate in protein folding in the endoplasmic reticulum (ER). CRT is a soluble ER lumenal protein, whereas CLNX is a transmembrane protein with a cytosolic domain that contains two consensus motifs for protein kinase (PK) C/proline- directed kinase (PDK) phosphorylation. Using confocal Ca(2+) imaging in Xenopus oocytes, we report here that coexpression of CLNX with sarco endoplasmic reticulum calcium ATPase (SERCA) 2b results in inhibition of intracellular Ca(2+) oscillations, suggesting a functional inhibition of the pump. By site-directed mutagenesis, we demonstrate that this interaction is regulated by a COOH-terminal serine residue (S562) in CLNX. Furthermore, inositol 1,4,5-trisphosphate- mediated Ca(2+) release results in a dephosphorylation of this residue. We also demonstrate by coimmunoprecipitation that CLNX physically interacts with the COOH terminus of SERCA2b and that after dephosphorylation treatment, this interaction is significantly reduced. Together, our results suggest that CRT is uniquely regulated by ER lumenal conditions, whereas CLNX is, in addition, regulated by the phosphorylation status of its cytosolic domain. The S562 residue in CLNX acts as a molecular switch that regulates the interaction of the chaperone with SERCA2b, thereby affecting Ca(2+) signaling and controlling Ca(2+)-sensitive chaperone functions in the ER.

Indexed as

Calcium SignalingAmino Acid SequenceAnimalsCalciumCalcium-Binding ProteinsCalcium-Transporting ATPasesCalnexinCalreticulinEndoplasmic ReticulumInositol 1,4,5-TrisphosphateMicroscopy, FluorescenceMolecular Sequence DataMutagenesis, Site-DirectedOocytesPhosphorylationProtein BindingCalciumCalcium-Binding ProteinsCalcium-Transporting ATPasesCalnexinCalreticulinInositol 1,4,5-TrisphosphateRibonucleoproteins

Identifiers

PMID10851021
PMCPMC2175122
OpenAlexW2133624980

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.