Date of Award

6-2014

Document Type

Open Access

Degree Name

Bachelor of Science

Department

Biology

First Advisor

Brian Cohen

Language

English

Keywords

protein, expression, hormone, receptor

Abstract

The human FSH receptor is a g protein-coupled receptor (GPCR) expressed on the surface of granulosa cells in the ovary and Sertoli cells in the testes. FSHR has a sequence of amino acids consistent with a caveolin interaction motif (φXφXXXXφXXφ) found between amino acids 479-489 in the primary receptor sequence in the putative 4th transmembrane domain. Caveolin is a protein found in cell membrane micro domains such as lipid rafts. These densely packed regions of the membrane are enriched for sphingolipids and cholesterol and are thought to be involved in signal transduction. Caveolin can be found in caveolae, flask-like structures which are a specific type of lipid raft, or in non-caveolae lipid rafts. Although the receptor has this motif, it was unknown if hFSHR biochemically interacted with caveolin. To test this hypothesis, hFSHR was isolated by immunoprecipitiation from HEK-293 cells stably transfected with hFSHR cDNA. Analysis by western blot of co-immunoprecipitated proteins revealed the presence of caveolin-1. Together these results suggest that caveolin-1 plays an important role in cell signaling by sequestering hFSHR into lipid rafts for normal receptor function.

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