Evidence map›Paper›PMID 38786982›Full record

ArticleJournal of cell science2024

KRAP regulates mitochondrial Ca2+ uptake by licensing IP3 receptor activity and stabilizing ER-mitochondrial junctions.

Peace Atakpa-Adaji, Adelina Ivanova, Karolina Kujawa, Colin W Taylor

Abstract read
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In one paragraph

Article in Journal of cell science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Review
  2. Caffeic Acid Inhibits Degranulation, Cytokine Secretions, andInternational journal of molecular sciences · 2025
    Article
  3. Review
  4. Article
  5. Review
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

4 authors.

Peace Atakpa-AdajiDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK.ORCID 0000-0002-9398-7750
Adelina IvanovaDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK.ORCID 0000-0001-6388-8279
Karolina KujawaDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK.ORCID 0009-0008-9773-5674
Colin W TaylorDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK.ORCID 0000-0001-7771-1044

Funding

Biotechnology and Biological Sciences Research Council BB/TO/12986/1Cambridge TrustCambridge Trust NAEmmanuel College, University of CambridgeEmmanuel College, University of Cambridge NAUniversity of CambridgeWellcomeWellcome Trust
6 · The paper itself

Abstract

Inositol 1,4,5-trisphosphate (IP3) receptors (IP3Rs) are high-conductance channels that allow the regulated redistribution of Ca2+ from the endoplasmic reticulum (ER) to the cytosol and, at specialized membrane contact sites (MCSs), to other organelles. Only a subset of IP3Rs release Ca2+ to the cytosol in response to IP3. These 'licensed' IP3Rs are associated with Kras-induced actin-interacting protein (KRAP, also known as ITPRID2) beneath the plasma membrane. It is unclear whether KRAP regulates IP3Rs at MCSs. We show, using simultaneous measurements of Ca2+ concentration in the cytosol and mitochondrial matrix, that KRAP also licenses IP3Rs to release Ca2+ to mitochondria. Loss of KRAP abolishes cytosolic and mitochondrial Ca2+ signals evoked by stimulation of IP3Rs via endogenous receptors. KRAP is located at ER-mitochondrial membrane contact sites (ERMCSs) populated by IP3R clusters. Using a proximity ligation assay between IP3R and voltage-dependent anion channel 1 (VDAC1), we show that loss of KRAP reduces the number of ERMCSs. We conclude that KRAP regulates Ca2+ transfer from IP3Rs to mitochondria by both licensing IP3R activity and stabilizing ERMCSs.

Indexed as

CalciumEndoplasmic ReticulumInositol 1,4,5-Trisphosphate ReceptorsMitochondriaAnimalsCalcium SignalingCytosolHeLa CellsHumansLectins, C-TypeMembrane ProteinsMicrofilament ProteinsMitochondrial MembranesVoltage-Dependent Anion Channel 1CalciumCLECL1 protein, humanInositol 1,4,5-Trisphosphate ReceptorsITPRID2 protein, humanLectins, C-TypeMembrane ProteinsMicrofilament ProteinsVoltage-Dependent Anion Channel 1Ca2+Endoplasmic reticulumHeLa cellHistamineIP3 receptorKRAPMCUMembrane contact siteMitochondriaProximity ligation assayVDAC1

Identifiers

PMID38786982
PMCPMC11234384

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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.