Evidence map›Paper›PMID 26083340›Full record

ArticleCell cycle (Georgetown, Tex.)2015

Reinforcing the LINC complex connection to actin filaments: the role of FHOD1 in TAN line formation and nuclear movement.

Susumu Antoku, Ruijun Zhu, Stefan Kutscheidt, Oliver T Fackler, Gregg G Gundersen

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Mechanically-induced Septin Networks Protect Nuclear Integrity.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Molecular-Level Interactions between Engineered Materials and Cells.International journal of molecular sciences · 2019
    Review
  11. Nuclear positioning in migrating fibroblasts.Seminars in cell & developmental biology · 2018
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. 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

5 authors at 4 institutions in 2 countries.

Susumu Antokua Department of Pathology & Cell Biology ; Columbia University ; New York , NY USA.
Ruijun Zhu
Stefan Kutscheidt
Oliver T Fackler
Gregg G Gundersen
New York Proton Center · USColumbia University · USHeidelberg University · USHeidelberg University · DE

Funding

Role of Nucleo-cytoskeleton Interactions in Cell MigrationR01GM099481 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GUNDERSEN, GREGG G · 2011 to 2019
$2.9M
Nucleocytoplasmic Interactions and Dynamics in Emery-Dreifuss Muscular DystrophyR56NS059352 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GUNDERSEN, GREGG G, WORMAN, HOWARD J · 2014 to 2014
$522k
NIGMS NIH HHS GM 099481NIGMS NIH HHS R01 GM099481NINDS NIH HHS NS05935
6 · The paper itself

Abstract

Positioning the nucleus is critical for many cellular processes including cell division, migration and differentiation. The linker of nucleoskeleton and cytoskeleton (LINC) complex spans the inner and outer nuclear membranes and has emerged as a major factor in connecting the nucleus to the cytoskeleton for movement and positioning. Recently, we discovered that the diaphanous formin family member FHOD1 interacts with the LINC complex component nesprin-2 giant (nesprin-2G) and that this interaction plays essential roles in the formation of transmembrane actin-dependent nuclear (TAN) lines and nuclear movement during cell polarization in fibroblasts. We found that FHOD1 strengthens the connection between nesprin-2G and rearward moving dorsal actin cables by providing a second site of interaction between nesprin-2G and the actin cable. These results indicate that the LINC complex connection to the actin cytoskeleton can be enhanced by cytoplasmic factors and suggest a new model for TAN line formation. We discuss how the nesprin-2G-FHOD1 interaction may be regulated and its possible functional significance for development and disease.

Indexed as

Actin CytoskeletonAnimalsCell NucleusFetal ProteinsForminsHEK293 CellsHumansMiceMicrofilament ProteinsNerve Tissue ProteinsNIH 3T3 CellsNuclear ProteinsFetal ProteinsFHOD1 protein, mouseForminsMicrofilament ProteinsNerve Tissue ProteinsNuclear ProteinsSyne2 protein, mouseABS, actin binding siteactin filamentsANC-1, Syne homologyCH, calponin homologyDAD, diaphanous autoregulatory domainDID, diaphanous inhibitory domainDRF, diaphanous related forminEDMD, Emery-Dreifuss muscular dystrophyEmery-Dreifuss muscular dystrophyFH, formin homologyFHOD1forminGBD, GTPase binding domainGFP-mN2G, GFP-mini-nesprin-2GKASH, KlarsichtLINC ComplexLINC, linker of nucleoskeleton and cytoskeletonLPA, lysophosphatidic acidnesprinnesprin-2G, nesprin-2 giantnuclear movementSR, spectrin repeatTAN linesTAN lines, transmembrane actin-dependent nuclear lines

Identifiers

PMID26083340
PMCPMC4614392
OpenAlexW1605554992

What OpenQuestion holds

Textmetadata
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.