Evidence map›Paper›PMID 32211895›Full record

ArticleThe Journal of cell biology2020

Differential turnover of Nup188 controls its levels at centrosomes and role in centriole duplication.

Nidhi Vishnoi, Karthigeyan Dhanasekeran, Madeleine Chalfant, Ivan Surovstev, Mustafa K Khokha, C Patrick Lusk

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  7. Article
  8. Non-classical functions of nuclear pore proteins in ciliopathy.Frontiers in molecular biosciences · 2023
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
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

6 authors at 2 institutions in 1 country.

Nidhi VishnoiDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Karthigeyan DhanasekeranDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Madeleine ChalfantDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Ivan SurovstevDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Mustafa K KhokhaPediatric Genomics Discovery Program, Departments of Pediatrics and Genetics, Yale School of Medicine, New Haven, CT.
C Patrick LuskDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Yale University · USPediatrics and Genetics · US

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
New Mechanisms of Heterotaxy and Congenital Heart Disease: Nucleoporins at CiliaR01HL124402 · NHLBI · YALE UNIVERSITY · PI KHOKHA, MUSTAFA K, LUSK, CHARLES PATRICK · 2015 to 2022
$5.5M
Determining the role of nucleoporins in ciliogenesis and heart developmentF31HL134272 · NHLBI · YALE UNIVERSITY · PI CHALFANT, MADELEINE · 2016 to 2018
$101k
NCATS NIH HHS UL1 TR001863NHLBI NIH HHS F31 HL134272NHLBI NIH HHS R01 HL124402NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

NUP188 encodes a scaffold component of the nuclear pore complex (NPC) and has been implicated as a congenital heart disease gene through an ill-defined function at centrioles. Here, we explore the mechanisms that physically and functionally segregate Nup188 between the pericentriolar material (PCM) and NPCs. Pulse-chase fluorescent labeling indicates that Nup188 populates centrosomes with newly synthesized protein that does not exchange with NPCs even after mitotic NPC breakdown. In addition, the steady-state levels of Nup188 are controlled by the sensitivity of the PCM pool, but not the NPC pool, to proteasomal degradation. Proximity-labeling and super-resolution microscopy show that Nup188 is vicinal to the inner core of the interphase centrosome. Consistent with this, we demonstrate direct binding between Nup188 and Cep152. We further show that Nup188 functions in centriole duplication at or upstream of Sas6 loading. Together, our data establish Nup188 as a component of PCM needed to duplicate the centriole with implications for congenital heart disease mechanisms.

Indexed as

MitosisCell Cycle ProteinsCentriolesCentrosomeHeLa CellsHumansNuclear Pore Complex ProteinsProteasome Endopeptidase ComplexProtein BindingProteolysisSignal TransductionTime FactorsCell Cycle ProteinsCEP152 protein, humanNuclear Pore Complex ProteinsNUP188 protein, humanProteasome Endopeptidase Complex

Identifiers

PMID32211895
PMCPMC7055002
OpenAlexW3008309284

What Socratic 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 Socratic graph.