Evidence map›Paper›PMID 34821358›Full record

ArticleJournal of cell science2022

The endoplasmic reticulum-plasma membrane tethering protein TMEM24 is a regulator of cellular Ca2+ homeostasis.

Beichen Xie, Styliani Panagiotou, Jing Cen, Patrick Gilon, Peter Bergsten, Olof Idevall-Hagren

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
3.3field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Concerted transport and phosphorylation of diacylglycerol at ER-PM contact sites regulate phospholipid dynamics during stress.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. The Extended Synaptotagmins ofPlants (Basel, Switzerland) · 2025
    Review
  9. Article
  10. Article
  11. Imaging and proteomics toolkits for studying organelle contact sites.Frontiers in cell and developmental biology · 2024
    Review
  12. Article
  13. 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

6 authors at 2 institutions in 2 countries.

Beichen XieDepartment of Medical Cell Biology, Uppsala University, BMC Box 571, 75123 Uppsala, Sweden.
Styliani PanagiotouDepartment of Medical Cell Biology, Uppsala University, BMC Box 571, 75123 Uppsala, Sweden.
Jing CenDepartment of Medical Cell Biology, Uppsala University, BMC Box 571, 75123 Uppsala, Sweden.
Patrick GilonPole of Endocrinology, Diabetes and Nutrition (EDIN), Institute of Experimental and Clinical Research (IREC), Université Catholique de Louvain, Avenue Hippocrate 55, B1.55.06 B-1200 Brussels, Belgium.
Peter BergstenDepartment of Medical Cell Biology, Uppsala University, BMC Box 571, 75123 Uppsala, Sweden.
Olof Idevall-HagrenDepartment of Medical Cell Biology, Uppsala University, BMC Box 571, 75123 Uppsala, Sweden.ORCID 0000-0002-0241-6304
Uppsala University · SEUCLouvain · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoplasmic reticulum (ER)-plasma membrane (PM) contacts are sites of lipid exchange and Ca2+ transport, and both lipid transport proteins and Ca2+ channels specifically accumulate at these locations. In pancreatic β-cells, both lipid and Ca2+ signaling are essential for insulin secretion. The recently characterized lipid transfer protein TMEM24 (also known as C2CD2L) dynamically localizes to ER-PM contact sites and provides phosphatidylinositol, a precursor of phosphatidylinositol-4-phosphate [PI(4)P] and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], to the PM. β-cells lacking TMEM24 exhibit markedly suppressed glucose-induced Ca2+ oscillations and insulin secretion, but the underlying mechanism is not known. We now show that TMEM24 only weakly interacts with the PM, and dissociates in response to both diacylglycerol and nanomolar elevations of cytosolic Ca2+. Loss of TMEM24 results in hyper-accumulation of Ca2+ in the ER and in excess Ca2+ entry into mitochondria, with resulting impairment in glucose-stimulated ATP production.

Indexed as

CalciumMembrane ProteinsCell MembraneEndoplasmic ReticulumHomeostasisCalciumMembrane ProteinsCa2+Insulin secretionMembrane contact sitesMitochondriaPhosphoinositides

Identifiers

PMID34821358
PMCPMC8729788
OpenAlexW3215098997

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.