Evidence map›Paper›PMID 36139365›Full record

ArticleCells2022

The Adhesion GPCR VLGR1/ADGRV1 Regulates the Ca

Jacek Krzysko, Filip Maciag, Anna Mertens, Baran Enes Güler, Joshua Linnert, Karsten Boldt, Marius Ueffing, Kerstin Nagel-Wolfrum, Martin Heine, Uwe Wolfrum

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. 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
2.1field-weighted citation impact, top 13% 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, 25 citations in OpenAlex.

  1. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  2. Article
  3. Article
  4. Nonsense Mutation inInternational journal of molecular sciences · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
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  13. Review
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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

10 authors at 2 institutions in 1 country.

Jacek KrzyskoInstitute of Molecular Physiology (imP), Molecular Cell Biology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
Filip MaciagInstitute for Developmental Biology and Neurobiology (IDN), Functional Neurobiology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
Anna MertensInstitute of Molecular Physiology (imP), Molecular Cell Biology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
Baran Enes GülerInstitute of Molecular Physiology (imP), Molecular Cell Biology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
Joshua LinnertInstitute of Molecular Physiology (imP), Molecular Cell Biology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
Karsten BoldtInstitute for Ophthalmic Research, University of Tuebingen, 72076 Tuebingen, Germany.ORCID 0000-0002-2693-689X
Marius UeffingInstitute for Ophthalmic Research, University of Tuebingen, 72076 Tuebingen, Germany.ORCID 0000-0003-2209-2113
Kerstin Nagel-WolfrumInstitute of Molecular Physiology (imP), Molecular Cell Biology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
Martin HeineInstitute for Developmental Biology and Neurobiology (IDN), Functional Neurobiology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
Uwe WolfrumInstitute of Molecular Physiology (imP), Molecular Cell Biology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.ORCID 0000-0002-4756-5872
Johannes Gutenberg University Mainz · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The very large G protein-coupled receptor (VLGR1, ADGRV1) is the largest member of the adhesion GPCR family. Mutations in VLGR1 have been associated with the human Usher syndrome (USH), the most common form of inherited deaf-blindness as well as childhood absence epilepsy. VLGR1 was previously found as membrane-membrane adhesion complexes and focal adhesions. Affinity proteomics revealed that in the interactome of VLGR1, molecules are enriched that are associated with both the ER and mitochondria, as well as mitochondria-associated ER membranes (MAMs), a compartment at the contact sites of both organelles. We confirmed the interaction of VLGR1 with key proteins of MAMs by pull-down assays in vitro complemented by in situ proximity ligation assays in cells. Immunocytochemistry by light and electron microscopy demonstrated the localization of VLGR1 in MAMs. The absence of VLGR1 in tissues and cells derived from VLGR1-deficient mouse models resulted in alterations in the MAM architecture and in the dysregulation of the Ca

Indexed as

Endoplasmic ReticulumMitochondrial MembranesAnimalsChildHomeostasisHumansMiceMitochondriaadhesion GPCRCa2+ homeostasisCa2+ transient at ER and mitochondriamitochondria-associated ER membranes (MAM)mitochondria-endoplasmic reticulum contact sites (MERCS)

Identifiers

PMID36139365
PMCPMC9496679
OpenAlexW4295106690

What OpenQuestion holds

Textmetadata
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.