Evidence map›Paper›PMID 39982998›Full record

ArticleScience advances2025

Active microtubule-actin cross-talk mediated by a nesprin-2G-kinesin complex.

Natalie Sahabandu, Kyoko Okada, Aisha Khan, Daniel Elnatan, Daniel A Starr, Kassandra M Ori-McKenney, G W Luxton, Richard J McKenney

Abstract read
In one paragraph

Article in Science advances, 2025. 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
–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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Force-dependent structural dynamics of the giant nesprin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Review
  9. Article
  10. Review
  11. 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

8 authors.

Natalie SahabanduMolecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.ORCID 0009-0005-0129-2564
Kyoko OkadaMolecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.ORCID 0009-0009-3877-3774
Aisha KhanMolecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.ORCID 0009-0002-3265-8045
Daniel ElnatanMolecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.ORCID 0000-0002-8359-0522
Daniel A StarrMolecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.ORCID 0000-0001-7339-6606
Kassandra M Ori-McKenneyMolecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.ORCID 0000-0003-2051-2495
G W LuxtonMolecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.ORCID 0000-0002-6180-8906
Richard J McKenneyMolecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.ORCID 0000-0002-8423-0852

Funding

Coordination of molecular motor activity in intracellular transport and assembly of cytoskeletal architecture.R35GM124889 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Richard James McKenney · 2017 to 2026
$4.3M
Defining microtubule cytoskeleton regulatory pathways in development and diseaseR35GM133688 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Kassandra Marie Ori-McKenney · 2019 to 2026
$3.1M
Mechanisms of Nuclear MigrationR35GM134859 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI DANIEL A STARR · 2020 to 2026
$2.8M
NIGMS NIH HHS R35 GM124889NIGMS NIH HHS R35 GM133688NIGMS NIH HHS R35 GM134859
6 · The paper itself

Abstract

Nesprin-2 Giant (N2G) is a large integral membrane protein that physically connects the nucleus to the cytoskeleton, but how N2G performs this activity to maintain nuclear positioning and drive nuclear movement is unclear. This study investigates N2G's role in nucleocytoskeletal coupling, a process critical for cellular function and development. We uncover multiple roles for N2G, including its activity as an F-actin bundler, an adapter that activates kinesin-1 motors, and a mediator of cytoskeletal cross-talk. Notably, N2G directly links kinesin-1 to F-actin, enabling the transport of actin filaments along microtubule tracks, establishing active cross-talk between the actin and microtubule cytoskeletons. These findings provide crucial insights into nuclear movement, advancing our understanding of fundamental cellular processes and their implications in development and disease.

Indexed as

ActinsKinesinsMicrofilament ProteinsMicrotubulesNerve Tissue ProteinsNuclear ProteinsActin CytoskeletonAnimalsCell NucleusHumansProtein BindingActinsKinesinsMicrofilament ProteinsNerve Tissue ProteinsNuclear Proteins

Identifiers

PMID39982998
PMCPMC11844729

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.