Evidence map›Paper›PMID 36650170›Full record

ArticleNature communications2023

Dynamics of CLIMP-63 S-acylation control ER morphology.

Patrick A Sandoz, Robin A Denhardt-Eriksson, Laurence Abrami, Luciano A Abriata, Gard Spreemann, Catherine Maclachlan, Sylvia Ho, Béatrice Kunz, Kathryn Hess, Graham Knott and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

12 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Membrane Contact Sites in Proteostasis and ER Stress Response.Contact (Thousand Oaks (Ventura County, Calif.))
    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

13 authors at 2 institutions in 1 country.

Patrick A SandozGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.ORCID 0000-0002-8379-7267
Robin A Denhardt-ErikssonLaboratory of Computational Systems Biotechnology, EPFL, Lausanne, Switzerland.
Laurence AbramiGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.ORCID 0000-0002-1774-0481
Luciano A AbriataLaboratory for Biomolecular Modelling, Institute of Bioengineering, EPFL and Swiss Institute of Bioinformatics, Lausanne, Switzerland.ORCID 0000-0003-3087-8677
Gard SpreemannBrain Mind Institute, EPFL, Lausanne, Switzerland.ORCID 0000-0002-5945-0466
Catherine MaclachlanBioEM Facility, School of Life Sciences, EPFL, Lausanne, Switzerland.
Sylvia HoGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.ORCID 0000-0002-2969-7329
Béatrice KunzGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.
Kathryn HessBrain Mind Institute, EPFL, Lausanne, Switzerland.ORCID 0000-0003-2788-9754
Graham KnottBioEM Facility, School of Life Sciences, EPFL, Lausanne, Switzerland.ORCID 0000-0002-2956-9052
Francisco S MesquitaGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland. francisco.mesquita@epfl.ch.ORCID 0000-0002-3777-825X
Vassily HatzimanikatisLaboratory of Computational Systems Biotechnology, EPFL, Lausanne, Switzerland. vassily.hatzimanikatis@epfl.ch.ORCID 0000-0001-6432-4694
F Gisou van der GootGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland. gisou.vandergoot@epfl.ch.ORCID 0000-0002-8522-274X
École Polytechnique Fédérale de Lausanne · CHSIB Swiss Institute of Bioinformatics · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The complex architecture of the endoplasmic reticulum (ER) comprises distinct dynamic features, many at the nanoscale, that enable the coexistence of the nuclear envelope, regions of dense sheets and a branched tubular network that spans the cytoplasm. A key player in the formation of ER sheets is cytoskeleton-linking membrane protein 63 (CLIMP-63). The mechanisms by which CLIMP-63 coordinates ER structure remain elusive. Here, we address the impact of S-acylation, a reversible post-translational lipid modification, on CLIMP-63 cellular distribution and function. Combining native mass-spectrometry, with kinetic analysis of acylation and deacylation, and data-driven mathematical modelling, we obtain in-depth understanding of the CLIMP-63 life cycle. In the ER, it assembles into trimeric units. These occasionally exit the ER to reach the plasma membrane. However, the majority undergoes S-acylation by ZDHHC6 in the ER where they further assemble into highly stable super-complexes. Using super-resolution microscopy and focused ion beam electron microscopy, we show that CLIMP-63 acylation-deacylation controls the abundance and fenestration of ER sheets. Overall, this study uncovers a dynamic lipid post-translational regulation of ER architecture.

Indexed as

Endoplasmic ReticulumMembrane ProteinsAcylationKineticsLipidsLipidsMembrane Proteins

Identifiers

PMID36650170
PMCPMC9844198
OpenAlexW4317040560

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.