Evidence map›Paper›PMID 37490546›Full record

ArticleScience signaling2023

Structure of the photoreceptor synaptic assembly of the extracellular matrix protein pikachurin with the orphan receptor GPR179.

Dipak N Patil, Serena Pantalone, Yan Cao, Thibaut Laboute, Scott J Novick, Shikha Singh, Simone Savino, Silvia Faravelli, Francesca Magnani, Patrick R Griffin and 3 more

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

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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

13 authors at 4 institutions in 3 countries.

Dipak N PatilDepartment of Neuroscience, Herbert Wertheim UF Scripps Institute for Biomedical Innovation and Technology, University of Florida, Jupiter, FL 33458, USA.ORCID 0000-0003-1112-5557
Serena PantaloneArmenise-Harvard Laboratory of Structural Biology, Department of Biology and Biotechnology, University of Pavia, Via Ferrata, 9A, I-27100 Pavia, Italy.ORCID 0000-0002-7951-4690
Yan CaoDepartment of Neuroscience, Herbert Wertheim UF Scripps Institute for Biomedical Innovation and Technology, University of Florida, Jupiter, FL 33458, USA.ORCID 0000-0003-4902-2297
Thibaut LabouteDepartment of Neuroscience, Herbert Wertheim UF Scripps Institute for Biomedical Innovation and Technology, University of Florida, Jupiter, FL 33458, USA.ORCID 0000-0003-0870-1891
Scott J NovickDepartment of Molecular Medicine, Herbert Wertheim UF Scripps Institute for Biomedical Innovation & Technology, University of Florida, Jupiter, FL 33458, USA.ORCID 0000-0003-0213-3897
Shikha SinghDepartment of Biological Sciences, Columbia University New York, New York, NY 10027, USA.ORCID 0000-0003-0266-4241
Simone SavinoArmenise-Harvard Laboratory of Structural Biology, Department of Biology and Biotechnology, University of Pavia, Via Ferrata, 9A, I-27100 Pavia, Italy.ORCID 0000-0001-9505-3348
Silvia FaravelliArmenise-Harvard Laboratory of Structural Biology, Department of Biology and Biotechnology, University of Pavia, Via Ferrata, 9A, I-27100 Pavia, Italy.ORCID 0000-0001-7120-6370
Francesca MagnaniArmenise-Harvard Laboratory of Structural Biology, Department of Biology and Biotechnology, University of Pavia, Via Ferrata, 9A, I-27100 Pavia, Italy.ORCID 0000-0003-0812-9397
Patrick R GriffinDepartment of Molecular Medicine, Herbert Wertheim UF Scripps Institute for Biomedical Innovation & Technology, University of Florida, Jupiter, FL 33458, USA.
Appu K SinghDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur 208016, India.ORCID 0000-0002-2685-4018
Federico FornerisArmenise-Harvard Laboratory of Structural Biology, Department of Biology and Biotechnology, University of Pavia, Via Ferrata, 9A, I-27100 Pavia, Italy.ORCID 0000-0002-7818-1804
Kirill A MartemyanovDepartment of Neuroscience, Herbert Wertheim UF Scripps Institute for Biomedical Innovation and Technology, University of Florida, Jupiter, FL 33458, USA.ORCID 0000-0002-9925-7599
Scripps Research Institute · USUniversity of Pavia · ITColumbia University · USIndian Institute of Technology Kanpur · IN

Funding

Regulation of Signaling in the Retina by RGS ProteinsR01EY018139 · NEI · UNIVERSITY OF MINNESOTA · PI MARTEMYANOV, KIRILL A. · 2007 to 2025
$8.9M
Orphan Receptors in Regulation of Neuronal G Protein SignalingR01MH105482 · NIMH · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI Kirill A. Martemyanov · 2015 to 2026
$6.1M
Structural landscape of photoreceptor synapsesR01EY034339 · NEI · UNIVERSITY OF FLORIDA · PI MARTEMYANOV, KIRILL A., SINGH, APPU · 2022 to 2024
$1.4M
NCI NIH HHS HHSN261200800001ENEI NIH HHS R01 EY018139NEI NIH HHS R01 EY034339NIMH NIH HHS R01 MH105482
6 · The paper itself

Abstract

Precise synapse formation is essential for normal functioning of the nervous system. Retinal photoreceptors establish selective contacts with bipolar cells, aligning the neurotransmitter release apparatus with postsynaptic signaling cascades. This involves transsynaptic assembly between the dystroglycan-dystrophin complex on the photoreceptor and the orphan receptor GPR179 on the bipolar cell, which is mediated by the extracellular matrix protein pikachurin (also known as EGFLAM). This complex plays a critical role in the synaptic organization of photoreceptors and signal transmission, and mutations affecting its components cause blinding disorders in humans. Here, we investigated the structural organization and molecular mechanisms by which pikachurin orchestrates transsynaptic assembly and solved structures of the human pikachurin domains by x-ray crystallography and of the GPR179-pikachurin complex by single-particle, cryo-electron microscopy. The structures reveal molecular recognition principles of pikachurin by the Cache domains of GPR179 and show how the interaction is involved in the transsynaptic alignment of the signaling machinery. Together, these data provide a structural basis for understanding the synaptic organization of photoreceptors and ocular pathology.

Indexed as

Extracellular Matrix ProteinsSynapsesCarrier ProteinsCryoelectron MicroscopyHumansPhotoreceptor CellsReceptors, G-Protein-CoupledCarrier ProteinsExtracellular Matrix ProteinsGPR179 protein, humanReceptors, G-Protein-Coupled

Identifiers

PMID37490546
PMCPMC10561654
OpenAlexW4385258200

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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.