Evidence map›Paper›PMID 14970193›Full record

ArticleThe Journal of cell biology2004

Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein.

Yun Liang, Wei Yu, Yan Li, Zhenye Yang, Xiumin Yan, Qiongping Huang, Xueliang Zhu

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

68 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Nde1 Promotes Lis1-Mediated Activation of Dynein.bioRxiv : the preprint server for biology · 2023
    Article
  6. Article
  7. Ndel1 modulates dynein activation in two distinct ways.bioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Article
  10. Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022
    Review
  11. Article
  12. Activation and Regulation of Cytoplasmic Dynein.Trends in biochemical sciences · 2020
    Review
  13. Article
  14. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  15. Article
  16. Intermediate filaments and IF-associated proteins: from cell architecture to cell proliferation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Review
  17. Review
  18. Hepatic loss ofThe Journal of biological chemistry · 2018
    Article
  19. Article
  20. Article

8 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 1 country.

Yun LiangLaboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, China.
Wei Yu
Yan Li
Zhenye Yang
Xiumin Yan
Qiongping Huang
Xueliang Zhu
Center for Excellence in Molecular Cell Science · CNChinese Academy of Sciences · CNShanghai Institutes for Biological Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nudel and Lis1 appear to regulate cytoplasmic dynein in neuronal migration and mitosis through direct interactions. However, whether or not they regulate other functions of dynein remains elusive. Herein, overexpression of a Nudel mutant defective in association with either Lis1 or dynein heavy chain is shown to cause dispersions of membranous organelles whose trafficking depends on dynein. In contrast, the wild-type Nudel and the double mutant that binds to neither protein are much less effective. Time-lapse microscopy for lysosomes reveals significant reduction in both frequencies and velocities of their minus end-directed motions in cells expressing the dynein-binding defective mutant, whereas neither the durations of movement nor the plus end-directed motility is considerably altered. Moreover, silencing Nudel expression by RNA interference results in Golgi apparatus fragmentation and cell death. Together, it is concluded that Nudel is critical for dynein motor activity in membrane transport and possibly other cellular activities through interactions with both Lis1 and dynein heavy chain.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseAnimalsBinding SitesBiological TransportCarrier ProteinsCell LineCell MembraneDynactin ComplexDyneinsEndosomesGolgi ApparatusHumansLysosomesMicrotubule-Associated ProteinsMolecular Motor ProteinsProtein Binding1-Alkyl-2-acetylglycerophosphocholine EsteraseCarrier ProteinsDynactin ComplexDyneinsMicrotubule-Associated ProteinsMolecular Motor ProteinsNDEL1 protein, humanPAFAH1B1 protein, humanProtein IsoformsRecombinant Fusion Proteins

Identifiers

PMID14970193
PMCPMC2171987
OpenAlexW2164582507

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.