Evidence map›Paper›PMID 33873072›Full record

ArticleCell calcium2021

Insights into the molecular basis of the palmitoylation and depalmitoylation of NCX1.

Caglar Gök, Alice Main, Xing Gao, Zsombor Kerekes, Fiona Plain, Chien-Wen Kuo, Alan D Robertson, Niall J Fraser, William Fuller

Open access · hybridAbstract read
In one paragraph

Article in Cell calcium, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. An In Vivo Model of Estrogen Supplementation Concerning the Expression of CaJournal of cardiovascular development and disease · 2024
    Article
  7. Article
  8. Structural dynamics of NaCommunications biology · 2024
    Article
  9. Review
  10. Palmitoylation of solute carriers.Biochemical pharmacology · 2023
    Review
  11. Review
  12. Article
  13. Palmitoylation of Voltage-Gated Ion Channels.International journal of molecular sciences · 2022
    Review
  14. 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.

Caglar GökInstitute of Cardiovascular & Medical Sciences, Sir James Black Building, University of Glasgow, Glasgow, G12 8QQ, United Kingdom.
Alice MainInstitute of Cardiovascular & Medical Sciences, Sir James Black Building, University of Glasgow, Glasgow, G12 8QQ, United Kingdom.
Xing GaoInstitute of Cardiovascular & Medical Sciences, Sir James Black Building, University of Glasgow, Glasgow, G12 8QQ, United Kingdom.
Zsombor KerekesInstitute of Cardiovascular & Medical Sciences, Sir James Black Building, University of Glasgow, Glasgow, G12 8QQ, United Kingdom.
Fiona PlainSchool of Medicine, Ninewells Hospital, University of Dundee, Dundee, DD1 9SY, United Kingdom.
Chien-Wen KuoInstitute of Cardiovascular & Medical Sciences, Sir James Black Building, University of Glasgow, Glasgow, G12 8QQ, United Kingdom.
Alan D RobertsonInstitute of Cardiovascular & Medical Sciences, Sir James Black Building, University of Glasgow, Glasgow, G12 8QQ, United Kingdom.
Niall J FraserSchool of Medicine, Ninewells Hospital, University of Dundee, Dundee, DD1 9SY, United Kingdom.
William FullerInstitute of Cardiovascular & Medical Sciences, Sir James Black Building, University of Glasgow, Glasgow, G12 8QQ, United Kingdom. Electronic address: will.fuller@glasgow.ac.uk.
University of Glasgow · GBUniversity of Dundee · GB

Funding

British Heart Foundation FS/14/68/30988British Heart Foundation FS/17/14/32773British Heart Foundation PG/18/60/33957British Heart Foundation PG/19/5/34150British Heart Foundation RE/18/6/34217British Heart Foundation SP/16/3/32317
6 · The paper itself

Abstract

Catalyzed by zDHHC-PAT enzymes and reversed by thioesterases, protein palmitoylation is the only post-translational modification recognized to regulate the sodium/calcium exchanger NCX1. NCX1 palmitoylation occurs at a single site at position 739 in its large regulatory intracellular loop. An amphipathic ɑ-helix between residues 740-756 is a critical for NCX1 palmitoylation. Given the rich background of the structural elements involving in NCX1 palmitoylation, the molecular basis of NCX1 palmitoylation is still relatively poorly understood. Here we found that (1) the identity of palmitoylation machinery of NCX1 controls its spatial organization within the cell, (2) the NCX1 amphipathic ɑ-helix directly interacts with zDHHC-PATs, (3) NCX1 is still palmitoylated when it is arrested in either Golgi or ER, indicating that NCX1 is a substrate for multiple zDHHC-PATs, (4) the thioesterase APT1 but not APT2 as a part of NCX1-depalmitoylation machinery governs subcellular organization of NCX1, (5) APT1 catalyzes NCX1 depalmitoylation in the Golgi but not in the ER. We also report that NCX2 and NCX3 are dually palmitoylated, with important implications for substrate recognition and enzyme catalysis by zDHHC-PATs. Our results could support new molecular or pharmacological strategies targeting the NCX1 palmitoylation and depalmitoylation machinery.

Indexed as

APT1DepalmitoylationNCX1PalmitoylationThioesterasezDHHC-PATs

Identifiers

PMID33873072
PMCPMC8278489
OpenAlexW3156776493

What OpenQuestion holds

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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.