Evidence map›Paper›PMID 26649574›Full record

ArticlePloS one2015

Newly Characterized Region of CP190 Associates with Microtubules and Mediates Proper Spindle Morphology in Drosophila Stem Cells.

Karen M Plevock, Brian J Galletta, Kevin C Slep, Nasser M Rusan

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 25 citations in OpenAlex.

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  9. Mechanisms of Enhancer-Promoter Interactions in Higher Eukaryotes.International journal of molecular sciences · 2021
    Review
  10. Liposomal delivery of CRISPR/Cas9.Cancer gene therapy · 2020
    Review
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  15. Review
  16. Review
  17. 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 3 institutions in 1 country.

Karen M PlevockCell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, United State of America.
Brian J GallettaCell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, United State of America.
Kevin C SlepDepartment of Biology, University of North Carolina, Chapel Hill, North Carolina, 27599, United States of America.
Nasser M RusanCell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, United State of America.
University of North Carolina at Chapel Hill · USNational Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Regulating Centrosome Duplication and MaturationZIAHL006104 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI RUSAN, NASSER · 2011 to 2021
$8.6M
MOLECULAR AND CELLULAR BIOPHYSICS TRAINING PROGRAMT32GM008570 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A, SLEP, KEVIN C · 1995 to 2022
$5.1M
Molecular Mechanisms of Cytoskeletal RegulatorsR01GM094415 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROGERS, STEPHEN, SLEP, KEVIN C · 2011 to 2014
$1.1M
Intramural NIH HHS ZIA HL006104NIGMS NIH HHS R01 GM094415NIGMS NIH HHS T32 GM008570
6 · The paper itself

Abstract

CP190 is a large, multi-domain protein, first identified as a centrosome protein with oscillatory localization over the course of the cell cycle. During interphase it has a well-established role within the nucleus as a chromatin insulator. Upon nuclear envelope breakdown, there is a striking redistribution of CP190 to centrosomes and the mitotic spindle, in addition to the population at chromosomes. Here, we investigate CP190 in detail by performing domain analysis in cultured Drosophila S2 cells combined with protein structure determination by X-ray crystallography, in vitro biochemical characterization, and in vivo fixed and live imaging of cp190 mutant flies. Our analysis of CP190 identifies a novel N-terminal centrosome and microtubule (MT) targeting region, sufficient for spindle localization. This region consists of a highly conserved BTB domain and a linker region that serves as the MT binding domain. We present the 2.5 Å resolution structure of the CP190 N-terminal 126 amino acids, which adopts a canonical BTB domain fold and exists as a stable dimer in solution. The ability of the linker region to robustly localize to MTs requires BTB domain-mediated dimerization. Deletion of the linker region using CRISPR significantly alters spindle morphology and leads to DNA segregation errors in the developing Drosophila brain neuroblasts. Collectively, we highlight a multivalent MT-binding architecture in CP190, which confers distinct subcellular cytoskeletal localization and function during mitosis.

Indexed as

AnimalsCell NucleusCentrosomeChromosomesChromosome SegregationClustered Regularly Interspaced Short Palindromic RepeatsCrystallography, X-RayDNADrosophila melanogasterDrosophila ProteinsMicrotubule-Associated ProteinsMicrotubulesMitosisNuclear ProteinsSpindle ApparatusStem CellsCP190 protein, DrosophilaDNADrosophila ProteinsMicrotubule-Associated ProteinsNuclear Proteins

Identifiers

PMID26649574
PMCPMC4674064
OpenAlexW2191512761

What OpenQuestion holds

Textmetadata
LicenceCC0
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.