Evidence map›Paper›PMID 21056974›Full record

ArticleThe Journal of biological chemistry2011

Identification of a novel dynein binding domain in nudel essential for spindle pole organization in Xenopus egg extract.

Shusheng Wang, Yixian Zheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

45 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. CCSer2 gates dynein activity at the cell periphery.The Journal of cell biology · 2025
    Article
  4. Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Nde1 Promotes Lis1-Mediated Activation of Dynein.bioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Ndel1 modulates dynein activation in two distinct ways.bioRxiv : the preprint server for biology · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022
    Review
  14. Article
  15. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  16. Article
  17. Dynein activators and adaptors at a glance.Journal of cell science · 2019
    Review
  18. Article
  19. Article
  20. The cytoplasmic dynein transport machinery and its many cargoes.Nature reviews. Molecular cell biology · 2018
    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.

Shusheng WangDepartment of Embryology, Carnegie Institution for Science and Howard Hughes Medical Institute, Baltimore, Maryland 21218, USA.
Yixian Zheng
Carnegie Institution for Science · US

Funding

The function and assembly of the lamin-B spindle sheathR01GM056312 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI ZHENG, YIXIAN · 1997 to 2014
$2.7M
Howard Hughes Medical InstituteNIGMS NIH HHS GM56312NIGMS NIH HHS R01 GM056312
6 · The paper itself

Abstract

The nuclear distribution protein E (NudE) and nuclear distribution protein E-like (Nudel or Ndel1) interact with both lissencephaly 1 (Lis1) and dynein. These interactions are thought to be essential for dynein function. Previous studies have shown that the highly conserved N terminus of NudE/Nudel directly binds to Lis1, and such binding is critical for dynein activity. By contrast, although the C terminus of NudE/Nudel was reported to bind to dynein, the functional significance of this binding has remained unclear. Using the sperm-mediated spindle assembly assay in Xenopus egg extracts and extensive mutagenesis studies, we have identified a highly conserved dynein binding domain within the first 80 amino acids of Nudel. We further demonstrate that the dynein intermediate chain in the dynein complex is directly involved in this interaction. Importantly, we show that both the dynein and Lis1 binding domains of Nudel are required for spindle pole organization. Finally, we report that spindle defects caused by immuno-depletion of Nudel could be rescued by a 1-fold increase of Lis1 concentration in Xenopus egg extracts. This suggests that an important function of the N terminus of Nudel is to facilitate the interaction between Lis1 and dynein during spindle assembly. Together, our findings open up new avenues to further decipher the mechanism of dynein regulation by Nudel and Lis1.

Indexed as

XenopusAmino Acid SequenceAnimalsCell ExtractsCytoskeletal ProteinsDyneinsHumansMicrotubule-Associated ProteinsMolecular Sequence DataNuclear ProteinsOvumProtein BindingXenopus ProteinsCell ExtractsCytoskeletal ProteinsDyneinsMicrotubule-Associated ProteinsNdel1 protein, XenopusNuclear ProteinsXenopus Proteins

Identifiers

PMID21056974
PMCPMC3013018
OpenAlexW2026353278

What OpenQuestion 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 OpenQuestion graph.