ArticleCells2021
Trace Amine-Associated Receptor 1 Trafficking to Cilia of Thyroid Epithelial Cells.
Article in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Localization, trafficking, and signaling of trace amine-associated receptor 2 in mouse neuroblastoma cells.Cellular signalling · 2026Article
- The role of the primary cilium in thyroid function and dysfunction with implications for thyroid disease.Histochemistry and cell biology · 2025Review
- CU Cilia - an application for image analysis by machine learning - reveals significance of cysteine cathepsin K activity for primary cilia of human thyroid epithelial cells.Frontiers in endocrinology · 2025Article
- Characterization of primary cilia in different epithelial cells of thyroid gland.Histochemistry and cell biology · 2024Article
- Investigations on Primary Cilia of Nthy-ori 3-1 Cells upon Cysteine Cathepsin Inhibition or Thyrotropin Stimulation.International journal of molecular sciences · 2023Article
- Evaluation of Approach to a Conspecific and Blood Biochemical Parameters in TAAR1 Knockout Mice.Brain sciences · 2022Article
- TAAR1 Expression in Human Macrophages and Brain Tissue: A Potential Novel Facet of MS Neuroinflammation.International journal of molecular sciences · 2021Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Trace amine-associated receptor 1 (rodent Taar1/human TAAR1) is a G protein-coupled receptor that is mainly recognized for its functions in neuromodulation. Previous in vitro studies suggested that Taar1 may signal from intracellular compartments. However, we have shown Taar1 to localize apically and on ciliary extensions in rodent thyrocytes, suggesting that at least in the thyroid, Taar1 may signal from the cilia at the apical plasma membrane domain of thyrocytes in situ, where it is exposed to the content of the follicle lumen containing putative Taar1 ligands. This study was designed to explore mouse Taar1 (mTaar1) trafficking, heterologously expressed in human and rat thyroid cell lines in order to establish an in vitro system in which Taar1 signaling from the cell surface can be studied in future. The results showed that chimeric mTaar1-EGFP traffics to the apical cell surface and localizes particularly to spherical structures of polarized thyroid cells, procilia, and primary cilia upon serum-starvation. Moreover, mTaar1-EGFP appears to form high molecular mass forms, possibly homodimers and tetramers, in stably expressing human thyroid cell lines. However, only monomeric mTaar1-EGFP was cell surface biotinylated in polarized human thyrocytes. In polarized rat thyrocytes, mTaar1-EGFP is retained in the endoplasmic reticulum, while cilia were reached by mTaar1-EGFP transiently co-expressed in combination with an HA-tagged construct of the related mTaar5. We conclude that Taar1 trafficking to cilia depends on their integrity. The results further suggest that an in vitro cell model was established that recapitulates Taar1 trafficking in thyrocytes in situ, in principle, and will enable studying Taar1 signaling in future, thus extending our general understanding of its potential significance for thyroid autoregulation.
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