Evidence map›Paper›PMID 26337392›Full record

ArticleMolecular biology of the cell2015

MDM1 is a microtubule-binding protein that negatively regulates centriole duplication.

Daniel Van de Mark, Dong Kong, Jadranka Loncarek, Tim Stearns

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  6. Review
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  8. Article
  9. Investigating the Causal Effects of Exercise-Induced Genes on Sarcopenia.International journal of molecular sciences · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Exome Sequencing inFrontiers in genetics · 2019
    Article
  15. Article
  16. Article
  17. Anatomy of Mdm2 and Mdm4 in evolution.Journal of molecular cell biology · 2017
    Review
  18. 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

4 authors at 2 institutions in 1 country.

Daniel Van de MarkDepartment of Biology, Stanford University, Stanford, CA 94305.
Dong KongLaboratory of Protein Dynamics and Signaling, Center for Cancer Research-Frederick, National Cancer Institute, National Institutes of Health, Frederick, MD 21702.
Jadranka LoncarekLaboratory of Protein Dynamics and Signaling, Center for Cancer Research-Frederick, National Cancer Institute, National Institutes of Health, Frederick, MD 21702.
Tim StearnsDepartment of Biology, Stanford University, Stanford, CA 94305 Department of Genetics, Stanford University School of Medicine, Stanford University, Stanford, CA 94305 stearns@stanford.eu.
National Institutes of Health · USStanford University · US

Funding

INSTITUTIONAL TRAINING GRANT IN GENOME SCIENCET32HG000044 · NHGRI · STANFORD UNIVERSITY · PI MICHAEL P. SNYDER · 1995 to 2026
$32.2M
GAMMA TUBULIN AND CENTROSOME STRUCTURE AND FUNCTIONR01GM052022 · NIGMS · STANFORD UNIVERSITY · PI STEARNS, TIM · 1995 to 2017
$6.5M
NHGRI NIH HHS 5 T32 HG000044NHGRI NIH HHS T32 HG000044NIGMS NIH HHS R01 GM052022NIGMS NIH HHS R01GM52022NIH HHS 1S10OD01227601
6 · The paper itself

Abstract

Mouse double-minute 1 (Mdm1) was originally identified as a gene amplified in transformed mouse cells and more recently as being highly up-regulated during differentiation of multiciliated epithelial cells, a specialized cell type having hundreds of centrioles and motile cilia. Here we show that the MDM1 protein localizes to centrioles of dividing cells and differentiating multiciliated cells. 3D-SIM microscopy showed that MDM1 is closely associated with the centriole barrel, likely residing in the centriole lumen. Overexpression of MDM1 suppressed centriole duplication, whereas depletion of MDM1 resulted in an increase in granular material that likely represents early intermediates in centriole formation. We show that MDM1 binds microtubules in vivo and in vitro. We identified a repeat motif in MDM1 that is required for efficient microtubule binding and found that these repeats are also present in CCSAP, another microtubule-binding protein. We propose that MDM1 is a negative regulator of centriole duplication and that its function is mediated through microtubule binding.

Indexed as

Amino Acid MotifsCarrier ProteinsCell CycleCell Cycle ProteinsCell DifferentiationCentriolesCentrosomeCiliaEpithelial CellsHEK293 CellsHumansMicrotubule-Associated ProteinsMicrotubulesNuclear ProteinsProtein Structure, TertiaryRNA, Small InterferingCarrier ProteinsCell Cycle ProteinsMicrotubule-Associated ProteinsNuclear ProteinsRNA, Small Interfering

Identifiers

PMID26337392
PMCPMC4626064
OpenAlexW2262912190

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.