Evidence map›Paper›PMID 33472039›Full record

ArticleStructure (London, England : 1993)2021

Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins.

Sing Mei Lim, Victor E Cruz, Susumu Antoku, Gregg G Gundersen, Thomas U Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2021. 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
0.7field-weighted citation impact, top 32% 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, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Force-dependent structural dynamics of the giant nesprin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024
    Article
  11. Article
  12. Review
  13. FHODs: Nuclear tethered formins for nuclear mechanotransduction.Frontiers in cell and developmental biology · 2023
    Review
  14. Article
  15. Mechanics and functional consequences of nuclear deformations.Nature reviews. Molecular cell biology · 2022
    Review
  16. A LINC between the nucleus and the cytoskeleton takes form(in).Structure (London, England : 1993) · 2021
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Sing Mei LimDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Victor E CruzDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Susumu AntokuDepartment of Pathology and Cell Biology, Columbia University, New York, NY 10032, USA.
Gregg G GundersenDepartment of Pathology and Cell Biology, Columbia University, New York, NY 10032, USA.
Thomas U SchwartzDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: tus@mit.edu.
Massachusetts Institute of Technology · USColumbia University · US

Funding

PRE-DOCTORAL TRAINING IN THE BIOLOGICAL SCIENCEST32GM007287 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P., KEATING, AMY E · 1985 to 2019
$40.8M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Cytoskeleton, Nucleus and Integrin Recycling in Cell MigrationR35GM136403 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GUNDERSEN, GREGG G · 2020 to 2024
$3.3M
Structure-Function of the Nuclear Envelope Bridge and its Role in LaminopathiesR01AR065484 · NIAMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SCHWARTZ, THOMAS · 2014 to 2018
$1.6M
NIAMS NIH HHS R01 AR065484NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R35 GM136403NIGMS NIH HHS T32 GM007287
6 · The paper itself

Abstract

The nuclear position in eukaryotes is controlled by a nucleo-cytoskeletal network, critical in cell differentiation, division, and movement. Forces are transmitted through conserved Linker of Nucleoskeleton and Cytoskeleton (LINC) complexes that traverse the nuclear envelope and engage on either side of the membrane with diverse binding partners. Nesprin-2-giant (Nes2G), a LINC element in the outer nuclear membrane, connects to the actin directly as well as through FHOD1, a formin primarily involved in actin bundling. Here, we report the crystal structure of Nes2G bound to FHOD1 and show that the presumed G-binding domain of FHOD1 is rather a spectrin repeat (SR) binding enhancer for the neighboring FH3 domain. The structure reveals that SR binding by FHOD1 is likely not regulated by the diaphanous-autoregulatory domain helix of FHOD1. Finally, we establish that Nes1G also has one FHOD1 binding SR, indicating that these abundant, giant Nesprins have overlapping functions in actin-bundle recruitment for nuclear movement.

Indexed as

Amino Acid MotifsAnimalsCrystallography, X-RayCytoskeletal ProteinsFetal ProteinsForminsHEK293 CellsHumansMiceMicrofilament ProteinsModels, MolecularNerve Tissue ProteinsNIH 3T3 CellsProtein BindingProtein ConformationProtein DomainsCytoskeletal ProteinsFetal ProteinsFHOD1 protein, humanForminsMicrofilament ProteinsNerve Tissue ProteinsSYNE1 protein, humanSYNE2 protein, humanactin bundlingcytoskeletondiaphanous-related formin homology domainFH3 domainformin homology domain protein FHOD1LINC complexnesprinnuclear movementnucleoskeletonspectrin repeattransmembrane actin-associated nuclear (TAN) lines

Identifiers

PMID33472039
PMCPMC9122090
OpenAlexW3123896195

What Socratic holds

Textmetadata
LicenceTDM
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.