Date of Award


Document Type

Open Access

Degree Name

Bachelor of Science



First Advisor

Brian Cohen




ceels, transfection, dna, caveolin, protein


Human follicle stimulating hormone (hFSH) is a hormone found in humans that is synthesized and secreted by the anterior pituitary and targets the ovaries and testes. This specificity of targeting is accomplished by the interaction of hFSH with its receptor (hFSHR) on target cells. hFSHR is a G protein-coupled receptor that localizes to domains in the cell membrane known as lipid rafts. The mechanism of translocation of the hFSHR into lipid rafts is unknown. Our hypothesis is that translocation occurs through interaction of hFSHR with the protein caveolin via a specific sequence in the hFSHR; a putative caveolin interaction motif (CIM). The canonical caveolin interaction motif, FXFXXXXFXXF, where F is any aromatic amino acid such as phenylalanine (F), tyrosine (Y) or tryptophan (W) is found in the fourth transmembrane domain of hFSHR in amino acids 479-489 (FAFAAALFPIF). Here, the 4 critical phenylalanine residues match the motif. The goal of the current research has been to produce stable cell lines expressing isoforms of hFSHR with one of each of the four phenylalanines mutated to leucine. The mutant receptors were expressed in the cells and qualitatively demonstrated normal signaling when stimulated by hFSH. Future studies will focus on analyzing quantitative measurement of signaling and the location of the mutant receptor on the cell surface. Understanding the caveolin interaction motif of hFSHR could give us better understanding of the mechanism of hFSHR localization to lipid rafts and may give insight into a novel way to regulate FSH signaling and function.