Evidence map›Paper›PMID 26601071›Full record

ArticleEuropean thyroid journal2015

Trace Amine-Associated Receptor 1 Localization at the Apical Plasma Membrane Domain of Fisher Rat Thyroid Epithelial Cells Is Confined to Cilia.

Joanna Szumska, Maria Qatato, Maren Rehders, Dagmar Führer, Heike Biebermann, David K Grandy, Josef Köhrle, Klaudia Brix

Open access · greenAbstract read
In one paragraph

Article in European thyroid journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  4. Article
  5. The role of primary cilia in thyroid diseases.Frontiers in endocrinology · 2023
    Review
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  16. G-Protein-Coupled Receptor Signaling in Cilia.Cold Spring Harbor perspectives in biology · 2017
    Review
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  18. 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

8 authors at 4 institutions in 2 countries.

Joanna SzumskaDepartment of Life Sciences and Chemistry, Jacobs University Bremen, Bremen, Germany.
Maria QatatoDepartment of Life Sciences and Chemistry, Jacobs University Bremen, Bremen, Germany.
Maren RehdersDepartment of Life Sciences and Chemistry, Jacobs University Bremen, Bremen, Germany.
Dagmar FührerDepartment of Endocrinology and Metabolism and Division of Laboratory Research, University of Duisburg-Essen, Essen, Germany.
Heike BiebermannInstitut für Experimentelle Pädiatrische Endokrinologie, Charité-Universitätsmedizin Berlin, Berlin, Germany.
David K GrandyDepartment of Physiology and Pharmacology, School of Medicine and the Knight Cardiovascular Institute, Oregon Health & Science University, Portland, Oreg., USA.
Josef KöhrleInstitut für Experimentelle Endokrinologie, Charité-Universitätsmedizin Berlin, Berlin, Germany.
Klaudia BrixDepartment of Life Sciences and Chemistry, Jacobs University Bremen, Bremen, Germany.
Constructor University · DECharité - Universitätsmedizin Berlin · DEOregon Health & Science University · USUniversity of Duisburg-Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe trace amine-associated receptor 1 (Taar1) is one member of the Taar family of G-protein-coupled receptors (GPCR) accepting various biogenic amines as ligands. It has been proposed that Taar1 mediates rapid, membrane-initiated effects of thyronamines, the endogenous decarboxylated and deiodinated relatives of the classical thyroid hormones T4 and T3.

objectivesAlthough the physiological actions of thyronamines in general and 3-iodothyronamine (T1AM) in particular are incompletely understood, studies published to date suggest that synthetic T1AM-activated Taar1 signaling antagonizes thyromimetic effects exerted by T3. However, the location of Taar1 is currently unknown.

methodsTo fill this gap in our knowledge we employed immunofluorescence microscopy and a polyclonal antibody to detect Taar1 protein expression in thyroid tissue from Fisher rats, wild-type and taar1-deficient mice, and in the polarized FRT cells.

resultsWith this approach we found that Taar1 is expressed in the membranes of subcellular compartments of the secretory pathway and on the apical plasma membrane of FRT cells. Three-dimensional analyses further revealed Taar1 immunoreactivity in cilial extensions of postconfluent FRT cell cultures that had formed follicle-like structures.

conclusionsThe results suggest Taar1 transport along the secretory pathway and its accumulation in the primary cilium of thyrocytes. These findings are of significance considering the increasing interest in the role of cilia in harboring functional GPCR. We hypothesize that thyronamines can reach and activate Taar1 in thyroid follicular epithelia by acting from within the thyroid follicle lumen, their potential site of synthesis, as part of a nonclassical mechanism of thyroid autoregulation.

Indexed as

G-protein-coupled receptorsTaar1Thyroid follicleThyroid glandThyroid hormonesThyronamines

Identifiers

PMID26601071
PMCPMC4640295
OpenAlexW617514144

What OpenQuestion holds

Textmetadata
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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.