Abstract
The follicle-stimulating hormone receptor (FSHR) plays a crucial role in reproduction. This structurally complex receptor is a member of the G-protein coupled receptor (GPCR) superfamily of membrane receptors. As with the other structurally similar glycoprotein hormone receptors (the thyroid-stimulating hormone and luteinizing hormone-chorionic gonadotropin hormone receptors), the FSHR is characterized by an extensive extracellular domain, where binding to FSH occurs, linked to the signal specificity subdomain or hinge region. This region is involved in ligand-stimulated receptor activation whereas the seven transmembrane domain is associated with receptor activation and transmission of the activation process to the intracellular loops comprised of amino acid sequences, which predicate coupling to effectors, interaction with adapter proteins, and triggering of downstream intracellular signaling. In this review, we describe the most important structural features of the FSHR intimately involved in regulation of FSHR function, including trafficking, dimerization, and oligomerization, ligand binding, agonist-stimulated activation, and signal transduction.
Highlights
The glycoprotein hormone (GPH) receptors (GPHR), are members of the highly conserved Class A subfamily of the G protein-coupled receptor (GPCR) superfamily [1,2,3,4,5]
GPCRs are 7-transmembrane-helix protein molecules that transmit intracellular effects through activating intracellular signaling mediated by members of the guanine-nucleotide-binding signal-transducing proteins (G proteins); they are characterized by a single polypeptide chain that traverses the lipid bilayer of the plasma membrane seven times, forming characteristic transmembrane α-helices linked by alternating extracellular and intracellular sequences or loops, with an extracellular amino-terminus end and an intracellular carboxyl-terminal tail (C-tail) of variable lengths
This review summarizes the information available on the relationship between structure and function of the FSH receptor (FSHR)
Summary
The glycoprotein hormone (GPH) receptors (GPHR), are members of the highly conserved Class A subfamily (or rhodopsin-like family) of the G protein-coupled receptor (GPCR) superfamily [1,2,3,4,5]. The ECD acts as an agonist upon ligand binding and activates the sequence 353FNPCEDIMGY362 located in the junction of the carboxyl-terminal end of the hinge region and the 7TMD helix 1, which function as an internal agonist unit (Figure 1B).
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