Evidence map›Paper›PMID 31553752›Full record

ArticlePloS one2019

NPHP proteins are binding partners of nucleoporins at the base of the primary cilium.

T Lynne Blasius, Daisuke Takao, Kristen J Verhey

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. 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
1.1field-weighted citation impact, top 20% 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, 22 citations in OpenAlex.

  1. Review
  2. Identification of divergentbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Non-classical functions of nuclear pore proteins in ciliopathy.Frontiers in molecular biosciences · 2023
    Review
  10. Review
  11. Article
  12. Review
  13. Structure and dynamics of photoreceptor sensory cilia.Pflugers Archiv : European journal of physiology · 2021
    Review
  14. 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

3 authors at 1 institution in 1 country.

T Lynne BlasiusDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
Daisuke TakaoDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.ORCID 0000-0001-6136-6733
Kristen J VerheyDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.ORCID 0000-0001-9329-4981
University of Michigan · US

Funding

Research BaseP30DK092926 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARY ELLEN MICHELE HEISLER, ADESUWA B OLOMU · 2011 to 2026
$10.0M
Structure and Function of the Ciliary Pore ComplexR01GM116204 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VERHEY, KRISTEN J., YANG, WEIDONG · 2015 to 2018
$2.1M
NIDDK NIH HHS P30 DK092926NIGMS NIH HHS R01 GM116204
6 · The paper itself

Abstract

Cilia are microtubule-based organelles that protrude from the surface of eukaryotic cells to generate motility and to sense and respond to environmental cues. In order to carry out these functions, the complement of proteins in the cilium must be specific for the organelle. Regulation of protein entry into primary cilia has been shown to utilize mechanisms and components of nuclear gating, including nucleoporins of the nuclear pore complex (NPC). We show that nucleoporins also localize to the base of motile cilia on the surface of trachea epithelial cells. How nucleoporins are anchored at the cilium base has been unclear as transmembrane nucleoporins, which anchor nucleoporins at the nuclear envelope, have not been found to localize at the cilium. Here we use the directed yeast two-hybrid assay to identify direct interactions between nucleoporins and nephronophthisis proteins (NPHPs) which localize to the cilium base and contribute to cilium assembly and identity. We validate NPHP-nucleoporin interactions in mammalian cells using the knocksideways assay and demonstrate that the interactions occur at the base of the primary cilium using bimolecular fluorescence complementation. We propose that NPHP proteins anchor nucleoporins at the base of primary cilia to regulate protein entry into the organelle.

Indexed as

AnimalsChlorocebus aethiopsCiliaCOS CellsEpithelial CellsIntravital MicroscopyMiceMicroscopy, FluorescenceNIH 3T3 CellsNuclear Pore Complex ProteinsProtein BindingRatsRespiratory MucosaTracheaTranscription FactorsTwo-Hybrid System TechniquesNuclear Pore Complex ProteinsTranscription Factors

Identifiers

PMID31553752
PMCPMC6760808
OpenAlexW2974945746

What OpenQuestion holds

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LicenceCC BY
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.