Evidence map›Paper›PMID 27534274›Full record

ArticleNature communications2016

The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate.

Qing Wei, Yingyi Zhang, Clementine Schouteden, Yuxia Zhang, Qing Zhang, Jinhong Dong, Veronika Wonesch, Kun Ling, Alexander Dammermann, Jinghua Hu

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. bioRxiv : the preprint server for biology · 2025
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  15. Prenatal genetic considerations in congenital ventriculomegaly and hydrocephalus.Child's nervous system : ChNS : official journal of the International Society for Pediatric Neurosurgery · 2020
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

10 authors.

Qing WeiDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Yingyi ZhangDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Clementine SchoutedenMax F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna, A-1030 Vienna, Austria.
Yuxia ZhangDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Qing ZhangDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Jinhong DongDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Veronika WoneschMax F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna, A-1030 Vienna, Austria.
Kun LingDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Alexander DammermannMax F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna, A-1030 Vienna, Austria.
Jinghua HuDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.

Funding

Pilot and FeasibilityP30DK090728 · NIDDK · MAYO CLINIC ROCHESTER · PI ROMERO, MICHAEL F. · 2010 to 2019
$11.8M
Molecular dissection of the ciliary gateR01DK099160 · NIDDK · MAYO CLINIC ROCHESTER · PI Jinghua Hu · 2014 to 2026
$4.0M
Exploration of the functions of the ciliopathy Arls in cilia.R01DK090038 · NIDDK · MAYO CLINIC ROCHESTER · PI HU, JINGHUA · 2011 to 2019
$3.1M
Phosphoinsitide signaling in Breast Epithelial Morphogenesis and MetastasisR01CA149039 · NCI · MAYO CLINIC ROCHESTER · PI LING, KUN · 2010 to 2014
$1.6M
Austrian Science Fund FWF Y 597NCI NIH HHS R01 CA149039NIDDK NIH HHS P30 DK090728NIDDK NIH HHS R01 DK090038NIDDK NIH HHS R01 DK099160
6 · The paper itself

Abstract

Transition fibres (TFs), together with the transition zone (TZ), are basal ciliary structures thought to be crucial for cilium biogenesis and function by acting as a ciliary gate to regulate selective protein entry and exit. Here we demonstrate that the centriolar and basal body protein HYLS-1, the C. elegans orthologue of hydrolethalus syndrome protein 1, is required for TF formation, TZ organization and ciliary gating. Loss of HYLS-1 compromises the docking and entry of intraflagellar transport (IFT) particles, ciliary gating for both membrane and soluble proteins, and axoneme assembly. Additional depletion of the TF component DYF-19 in hyls-1 mutants further exacerbates TZ anomalies and completely abrogates ciliogenesis. Our data support an important role for HYLS-1 and TFs in establishment of the ciliary gate and underline the importance of selective protein entry for cilia assembly.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCiliaFlagellaGene DeletionHand Deformities, CongenitalHeart Defects, CongenitalHydrocephalusModels, BiologicalOrganogenesisCaenorhabditis elegans ProteinsHYLS-1 protein, C elegans

Identifiers

PMID27534274
PMCPMC4992140

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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.