Evidence map›Paper›PMID 21911489›Full record

ArticleThe Journal of biological chemistry2011

Mutually exclusive cytoplasmic dynein regulation by NudE-Lis1 and dynactin.

Richard J McKenney, Sarah J Weil, Julian Scherer, Richard B Vallee

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 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

73 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. CCSer2 gates dynein activity at the cell periphery.The Journal of cell biology · 2025
    Article
  3. Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025
    Article
  4. CCSer2 gates dynein activity at the cell periphery.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Nde1 Promotes Lis1-Mediated Activation of Dynein.bioRxiv : the preprint server for biology · 2023
    Article
  13. Article
  14. Ndel1 modulates dynein activation in two distinct ways.bioRxiv : the preprint server for biology · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022
    Review
  19. Article
  20. Article

13 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

4 authors at 1 institution in 1 country.

Richard J McKenneyDepartment of Pathology and Cell Biology, Columbia University, New York, New York 10032, USA.
Sarah J Weil
Julian Scherer
Richard B Vallee
Columbia University · US

Funding

Motor Proteins in Brain DevelopmentR01HD040182 · NICHD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI VALLEE, RICHARD BERT · 2000 to 2016
$4.9M
MOLECULAR GENETICS OF CYTOPLASMIC DYNEINR37GM047434 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI VALLEE, RICHARD BERT · 1996 to 2006
$3.5M
MOLECULAR GENETICS OF CYTOPLASMIC DYNEINR01GM047434 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI VALLEE, RICHARD BERT · 1992 to 2010
$2.6M
NICHD NIH HHS HD40182NICHD NIH HHS R01 HD040182NIGMS NIH HHS GM47434NIGMS NIH HHS R01 GM047434NIGMS NIH HHS R37 GM047434
6 · The paper itself

Abstract

Cytoplasmic dynein is responsible for a wide range of cellular roles. How this single motor protein performs so many functions has remained a major outstanding question for many years. Part of the answer is thought to lie in the diversity of dynein regulators, but how the effects of these factors are coordinated in vivo remains unexplored. We previously found NudE to bind dynein through its light chain 8 (LC8) and intermediate chain (IC) subunits (1), the latter of which also mediates the dynein-dynactin interaction (2). We report here that NudE and dynactin bind to a common region within the IC, and compete for this site. We find LC8 to bind to a novel sequence within NudE, without detectably affecting the dynein-NudE interaction. We further find that commonly used dynein inhibitory reagents have broad effects on the interaction of dynein with its regulatory factors. Together these results reveal an unanticipated mechanism for preventing dual regulation of individual dynein molecules, and identify the IC as a nexus for regulatory interactions within the dynein complex.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseAnimalsBinding SitesCell Cycle ProteinsCytoplasmic DyneinsDynactin ComplexHumansMiceMicrotubule-Associated ProteinsNerve Tissue ProteinsProtein BindingRats1-Alkyl-2-acetylglycerophosphocholine EsteraseCell Cycle ProteinsCytoplasmic DyneinsDynactin ComplexDYNLL1 protein, humanMicrotubule-Associated ProteinsNde1 protein, humanNde1 protein, mouseNerve Tissue ProteinsPAFAH1B1 protein, humanPafah1b1 protein, mousePafah1b1 protein, rat

Identifiers

PMID21911489
PMCPMC3234784
OpenAlexW2003825836

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.