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Updated: Jul 14, 2026

High-throughput Screening for Chemical Modulators of Post-transcriptionally Regulated Genes
Published on: March 3, 2015
Modulation of TSHR signaling by posttranslational modifications
1Medical Department III, University of Leipzig, Ph.-Rosenthal-Str. 27, 04103 Leipzig, Germany.
Abstract:
Posttranslational modifications of seven transmembrane receptors (7TMRs) affect their function to a large extent. Many studies of glycosylation or phosphorylation of 7TMRs have shown that these modifications influence the cell-surface expression or signaling of the receptor. Recently, other types of posttranslational modifications of the thyrotropin-stimulating hormone receptor (TSHR) have been characterized, including sialylation and dimerization. Increased TSHR sialylation results in increased TSHR cell-surface expression. Furthermore, TSHR oligomerization and the probable modification of TSHR signaling in lipid rafts require further clarification with regard to their functional consequences. In addition to its known coupling to Galphas and Galphaq, and possibly other G proteins, the TSHR also couples to further signaling pathways, such as the mitogen-activated protein kinase (MAPK) pathway, which involves G-protein-coupled receptor kinases (GRKs) and arrestins. We discuss these emerging new findings and their implications for signaling of the TSHR.
Insights
Posttranslational modifications significantly impact seven transmembrane receptors (7TMRs) function. New research highlights sialylation and dimerization of the thyrotropin-stimulating hormone receptor (TSHR), influencing its cell-surface expression and signaling pathways.
Area of Science:
- Biochemistry
- Molecular Biology
- Endocrinology
Background:
- Seven transmembrane receptors (7TMRs) undergo posttranslational modifications (PTMs) like glycosylation and phosphorylation, affecting their function.
- Recent studies reveal novel PTMs for the thyrotropin-stimulating hormone receptor (TSHR), including sialylation and dimerization.
Purpose of the Study:
- To explore the functional consequences of emerging posttranslational modifications on the thyrotropin-stimulating hormone receptor (TSHR).
- To discuss the implications of TSHR sialylation, dimerization, and novel signaling pathways.
Main Methods:
- Characterization of novel posttranslational modifications of the TSHR.
- Analysis of TSHR cell-surface expression and signaling pathways.
Main Results:
- Increased sialylation of TSHR leads to enhanced cell-surface expression.
- TSHR oligomerization and potential signaling modifications within lipid rafts warrant further investigation.
- TSHR signaling involves G-protein-coupled receptor kinases (GRKs) and arrestins, impacting the mitogen-activated protein kinase (MAPK) pathway.
Conclusions:
- Emerging posttranslational modifications significantly influence TSHR function and signaling.
- Further research is needed to fully elucidate the role of TSHR oligomerization and lipid raft interactions in its signaling cascade.
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