Evidence map›Paper›PMID 37188462›Full record

ArticleLife science alliance2023

Disulfide bond in SUN2 regulates dynamic remodeling of LINC complexes at the nuclear envelope.

Rahul Sharma, Martin W Hetzer

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Life outside the LINC complex - Do SUN proteins have LINC-independent functions?BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. 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

2 authors at 1 institution in 1 country.

Rahul SharmaMolecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA, USA.ORCID https://orcid.org/0000-0003-4023-6109
Martin W HetzerMolecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA, USA martin.hetzer@ist.ac.at.ORCID https://orcid.org/0000-0002-2111-992X
Salk Institute for Biological Studies · US

Funding

The role of long-lived proteins in the survival of nerve cellsR01NS096786 · NINDS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI HETZER, MARTIN W · 2015 to 2019
$3.6M
NINDS NIH HHS R01 NS096786
6 · The paper itself

Abstract

The LINC complex tethers the cell nucleus to the cytoskeleton to regulate mechanical forces during cell migration, differentiation, and various diseases. The function of LINC complexes relies on the interaction between highly conserved SUN and KASH proteins that form higher-order assemblies capable of load bearing. These structural details have emerged from in vitro assembled LINC complexes; however, the principles of in vivo assembly remain obscure. Here, we report a conformation-specific SUN2 antibody as a tool to visualize LINC complex dynamics in situ. Using imaging, biochemical, and cellular methods, we find that conserved cysteines in SUN2 undergo KASH-dependent inter- and intra-molecular disulfide bond rearrangements. Disruption of the SUN2 terminal disulfide bond compromises SUN2 localization, turnover, LINC complex assembly in addition to cytoskeletal organization and cell migration. Moreover, using pharmacological and genetic perturbations, we identify components of the ER lumen as SUN2 cysteines redox state regulators. Overall, we provide evidence for SUN2 disulfide bond rearrangement as a physiologically relevant structural modification that regulates LINC complex functions.

Indexed as

Nuclear EnvelopeNuclear ProteinsAnimalsCytoskeletonDisulfidesMembrane ProteinsMiceMicrotubulesTelomere-Binding ProteinsDisulfidesMembrane ProteinsNuclear ProteinsSun2 protein, mouseTelomere-Binding Proteins

Identifiers

PMID37188462
PMCPMC10193101
OpenAlexW4376602648

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.