ArticleCurrent issues in molecular biology2025
The N-Linked Glycosylation Asn191 and Asn199 Sites Are Controlled Differently Between PKA Signal Transduction and pEKR1/2 Activity in Equine Follicle-Stimulating Hormone Receptor.
Article in Current issues in molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- β-Arrestin 1 Differentially Modulates cAMP and ERK Pathways Downstream of the FSH Receptor.Current issues in molecular biology · 2025Article
- New Sights into Bioinformatics of Gene Regulations and Structure.International journal of molecular sciences · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Equine follicle-stimulating hormone receptor (eFSHR) contains four extracellular N-linked glycosylation sites, which play important roles in agonist-induced signal transduction. Glycosylation regulates G protein-coupled receptor mechanisms by influencing folding, ligand binding, signaling, trafficking, and internalization. Here, we examined whether the glycosylated sites in eFSHR are necessary for cyclic adenosine monophosphate (cAMP) signal transduction and the phosphate extracellular signal-regulated kinase 1/2 (pERK1/2) response. We constructed mutants (N191Q, N199Q, N268Q, and N293Q) of the four N-linked glycosylation sites in eFSHR using site-directed mutagenesis. In wild-type (wt) eFSHR, the cAMP response gradually increased dose-dependently, displaying a strong response at the EC
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