Evidence map›Paper›PMID 12556484›Full record

ArticleMolecular and cellular biology2003

Human Nudel and NudE as regulators of cytoplasmic dynein in poleward protein transport along the mitotic spindle.

Xiumin Yan, Fang Li, Yun Liang, Yidong Shen, Xiangshan Zhao, Qiongping Huang, Xueliang Zhu

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

66 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Ndel1 modulates dynein activation in two distinct ways.bioRxiv : the preprint server for biology · 2023
    Article
  5. Article
  6. Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022
    Review
  7. Review
  8. Activation and Regulation of Cytoplasmic Dynein.Trends in biochemical sciences · 2020
    Review
  9. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Using mouse transgenic and human stem cell technologies to model genetic mutations associated with schizophrenia and autism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  17. Article
  18. Review
  19. Article
  20. Article

6 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.

Xiumin YanLaboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Fang Li
Yun Liang
Yidong Shen
Xiangshan Zhao
Qiongping Huang
Xueliang Zhu
Center for Excellence in Molecular Cell Science · CNShanghai Institutes for Biological Sciences · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Emerging evidence supports the idea that a signaling pathway containing orthologs of at least mammalian NudE and Nudel, Lis1, and cytoplasmic dynein is conserved for eukaryotic nuclear migration. In mammals, this pathway has profound impact on neuronal migration during development of the central nervous system. Lis1 and dynein are also involved in other cellular functions, such as mitosis. Here we show that Nudel also participates in a subset of dynein function in M phase. Nudel was specifically phosphorylated in M phase in its serine/threonine phosphorylation motifs, probably by Cdc2 and also Erk1 and -2. A fraction of Nudel bound to centrosomes strongly in interphase and localized to mitotic spindles in early M phase. By using mutants incapable of or simulating phosphorylation, we confirmed that phosphorylation of Nudel regulated the cell-cycle-dependent distribution, possibly by increasing its dissociation rate at the microtubule-organizing center. Moreover, phosphorylated Nudel or the phosphorylation-mimicking mutant bound Lis1 more efficiently. We further demonstrated that a Nudel mutant incapable of binding to Lis1 impaired the poleward movement of dynein and hence the dynein-mediated transport of kinetochore proteins to spindle poles along microtubules, a process contributing to inactivation of the spindle checkpoint in mitosis. These results point to the importance of Nudel-Lis1 interaction for the dynein activity in M phase and to a possible role of Nudel phosphorylation as facilitating such interaction. In addition, comparative studies suggest that NudE is also functionally related to its paralog, Nudel.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseAdenosine TriphosphateCDC2 Protein KinaseCell Cycle ProteinsCells, CulturedCentrosomeCytoplasmDyneinsFungal ProteinsHumansMicrotubule-Associated ProteinsMitogen-Activated Protein Kinase 1MitosisMutationPhosphorylationProtein Transport1-Alkyl-2-acetylglycerophosphocholine EsteraseAdenosine TriphosphateCDC2 Protein KinaseCell Cycle ProteinsDyneinsFungal ProteinsMicrotubule-Associated ProteinsMitogen-Activated Protein Kinase 1PAFAH1B1 protein, humanRO-11 protein, Neurospora crassa

Identifiers

PMID12556484
PMCPMC141156
OpenAlexW2106492464

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.