Evidence map›Paper›PMID 26485514›Full record

ArticlePLoS genetics2015

NINL and DZANK1 Co-function in Vesicle Transport and Are Essential for Photoreceptor Development in Zebrafish.

Margo Dona, Ruxandra Bachmann-Gagescu, Yves Texier, Grischa Toedt, Lisette Hetterschijt, Edith L Tonnaer, Theo A Peters, Sylvia E C van Beersum, Judith G M Bergboer, Nicola Horn and 11 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Integrative genomic and functional analyses reveal NINL as a modulator of tau aggregation.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  5. Article
  6. Nlp-dependent ER-to-Golgi transport.International journal of biological sciences · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Dynein activators and adaptors at a glance.Journal of cell science · 2019
    Review
  17. Article
  18. Review
  19. The cytoplasmic dynein transport machinery and its many cargoes.Nature reviews. Molecular cell biology · 2018
    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

21 authors at 6 institutions in 3 countries.

Margo DonaDepartment of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands.
Ruxandra Bachmann-GagescuInstitute of Molecular Life Sciences, University of Zurich, Zürich, Switzerland; Institute of Medical Genetics, University of Zurich, Zürich, Switzerland.
Yves TexierDivision of Experimental Ophthalmology, and Medical Proteome Center, Centre for Ophthalmology, Eberhard Karls University Tuebingen, Tübingen, Germany.
Grischa ToedtStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Lisette HetterschijtRadboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
Edith L TonnaerDepartment of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands.
Theo A PetersDepartment of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands.
Sylvia E C van BeersumRadboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
Judith G M BergboerDepartment of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
Nicola HornDivision of Experimental Ophthalmology, and Medical Proteome Center, Centre for Ophthalmology, Eberhard Karls University Tuebingen, Tübingen, Germany.
Erik de VriezeDepartment of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands.
Ralph W N SlijkermanDepartment of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands.
Jeroen van ReeuwijkRadboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
Gert FlikDepartment of Organismal Animal Physiology, Institute for Water and Wetland Research, Radboud University Nijmegen, Nijmegen, The Netherlands.
Jan E KeunenDepartment of Ophthalmology, Radboud University Medical Centre, Nijmegen, the Netherlands.
Marius UeffingDivision of Experimental Ophthalmology, and Medical Proteome Center, Centre for Ophthalmology, Eberhard Karls University Tuebingen, Tübingen, Germany.
Toby J GibsonStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Ronald RoepmanRadboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
Karsten BoldtDivision of Experimental Ophthalmology, and Medical Proteome Center, Centre for Ophthalmology, Eberhard Karls University Tuebingen, Tübingen, Germany.
Hannie KremerDepartment of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
Erwin van WijkDepartment of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, the Netherlands.
Radboud University Nijmegen · NLRadboud University Medical Center · NLSTZ eyetrial · DEEuropean Molecular Biology Laboratory · DERadboud Institute for Molecular Life Sciences · NLUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ciliopathies are Mendelian disorders caused by dysfunction of cilia, ubiquitous organelles involved in fluid propulsion (motile cilia) or signal transduction (primary cilia). Retinal dystrophy is a common phenotypic characteristic of ciliopathies since photoreceptor outer segments are specialized primary cilia. These ciliary structures heavily rely on intracellular minus-end directed transport of cargo, mediated at least in part by the cytoplasmic dynein 1 motor complex, for their formation, maintenance and function. Ninein-like protein (NINL) is known to associate with this motor complex and is an important interaction partner of the ciliopathy-associated proteins lebercilin, USH2A and CC2D2A. Here, we scrutinize the function of NINL with combined proteomic and zebrafish in vivo approaches. We identify Double Zinc Ribbon and Ankyrin Repeat domains 1 (DZANK1) as a novel interaction partner of NINL and show that loss of Ninl, Dzank1 or both synergistically leads to dysmorphic photoreceptor outer segments, accumulation of trans-Golgi-derived vesicles and mislocalization of Rhodopsin and Ush2a in zebrafish. In addition, retrograde melanosome transport is severely impaired in zebrafish lacking Ninl or Dzank1. We further demonstrate that NINL and DZANK1 are essential for intracellular dynein-based transport by associating with complementary subunits of the cytoplasmic dynein 1 motor complex, thus shedding light on the structure and stoichiometry of this important motor complex. Altogether, our results support a model in which the NINL-DZANK1 protein module is involved in the proper assembly and folding of the cytoplasmic dynein 1 motor complex in photoreceptor cells, a process essential for outer segment formation and function.

Indexed as

Photoreceptor Cells, VertebrateAnimalsBiological TransportCarrier ProteinsCiliaDyneinsHEK293 CellsHumansLarvaMicrotubule-Associated ProteinsNeurogenesisNuclear ProteinsProteomicsRetinaSignal TransductionZebrafishCarrier ProteinsDyneinsDZANK1 protein, zebrafishMicrotubule-Associated ProteinsNINL protein, humanNuclear ProteinsZebrafish Proteins

Identifiers

PMID26485514
PMCPMC4617706
OpenAlexW1788428843

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Registered trials

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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.