Evidence map›Paper›PMID 20019668›Full record

ArticleThe EMBO journal2010

mNUDC is required for plus-end-directed transport of cytoplasmic dynein and dynactins by kinesin-1.

Masami Yamada, Shiori Toba, Takako Takitoh, Yuko Yoshida, Daisuke Mori, Takeshi Nakamura, Atsuko H Iwane, Toshio Yanagida, Hiroshi Imai, Li-Yuan Yu-Lee and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.2field-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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. PCID2, a subunit of theRNA biology · 2021
    Article
  7. Review
  8. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  9. Article
  10. Cytoskeletal control of nuclear migration in neurons and non-neuronal cells.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. JIP3 Activates Kinesin-1 Motility to Promote Axon Elongation.The Journal of biological chemistry · 2015
    Article
  18. Article
  19. Article
  20. JIP1 mediates anterograde transport of Rab10 cargos during neuronal polarization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
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

13 authors at 7 institutions in 3 countries.

Masami YamadaDepartment of Genetic Disease Research, Graduate School of Medicine, Osaka City University, Osaka, Japan.
Shiori Toba
Takako Takitoh
Yuko Yoshida
Daisuke Mori
Takeshi Nakamura
Atsuko H Iwane
Toshio Yanagida
Hiroshi Imai
Li-Yuan Yu-Lee
Trina Schroer
Anthony Wynshaw-Boris
Shinji Hirotsune
Osaka City University · JPOsaka University · JPBaylor College of Medicine · USJohns Hopkins University · USKyoto University · JPSPring-8 · JPUniversity of California, San Francisco · US

Funding

Genetic Analysis of LIS1 Function in the MouseR01NS041030 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WYNSHAW-BORIS, ANTHONY J. · 2002 to 2009
$3.1M
Genetic Regulation of Neuronal MigrationR01HD047380 · NICHD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WYNSHAW-BORIS, ANTHONY J. · 2005 to 2009
$1.2M
NICHD NIH HHS HD47380NICHD NIH HHS R01 HD047380NINDS NIH HHS NS41030NINDS NIH HHS R01 NS041030
6 · The paper itself

Abstract

Lissencephaly is a devastating neurological disorder caused by defective neuronal migration. The LIS1 (or PAFAH1B1) gene was identified as the gene mutated in lissencephaly patients, and was found to regulate cytoplasmic dynein function and localization. In particular, LIS1 is essential for anterograde transport of cytoplasmic dynein as a part of the cytoplasmic dynein-LIS1-microtubule complex in a kinesin-1-dependent manner. However, the underlying mechanism by which a cytoplasmic dynein-LIS1-microtubule complex binds kinesin-1 is unknown. Here, we report that mNUDC (mammalian NUDC) interacts with kinesin-1 and is required for the anterograde transport of a cytoplasmic dynein complex by kinesin-1. mNUDC is also required for anterograde transport of a dynactin-containing complex. Inhibition of mNUDC severely suppressed anterograde transport of distinct cytoplasmic dynein and dynactin complexes, whereas motility of kinesin-1 remained intact. Reconstruction experiments clearly demonstrated that mNUDC mediates the interaction of the dynein or dynactin complex with kinesin-1 and supports their transport by kinesin-1. Our findings have uncovered an essential role of mNUDC for anterograde transport of dynein and dynactin by kinesin-1.

Indexed as

AnimalsBiological TransportCell Cycle ProteinsCell MembraneCells, CulturedCytoplasmCytoplasmic DyneinsDynactin ComplexGanglia, SpinalKinesinsMiceMicrotubule-Associated ProteinsModels, BiologicalNeuronsNuclear ProteinsProtein BindingCell Cycle ProteinsCytoplasmic DyneinsDynactin ComplexKinesinsMicrotubule-Associated ProteinsNuclear ProteinsNudc protein, mouseRNA, Small Interfering

Identifiers

PMID20019668
PMCPMC2830693
OpenAlexW2068156633

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.