Binding interactions of the Mannose 6-phosphate/Insulin-like growth factor 2 receptor subdomains
Advisor Information
Jodi Kreiling
Location
Dr. C.C. and Mabel L. Criss Library
Presentation Type
Poster
Start Date
6-3-2015 2:00 PM
End Date
6-3-2015 3:30 PM
Abstract
The mannose 6-phosphate/insulin-like growth factor 2 receptor (Man6P/IGF2 receptor) is a mammalian cell membrane receptor involved in the regulation of cellular growth and tumor suppression, making it a necessary component in cancer research studies. The Man6P/IGF2 receptor is composed of several subdomains that are thought to aid in dimerization and proper receptor function. The goal of this research was to determine whether triplet subdomains on each Man6P/IGF2 receptor associate for optimal receptor function, and whether the strength of the interactions between two associating receptors is directly correlated with its molecular-binding abilities. In these studies, we were successful in preparing a MycHis tagged construct of the 7-9 subdomain of the Man6P/IGF2 receptor, confirming protein expression of the construct in cultured mammalian cells, and confirming protein co-expression of 7- 9MycHis with other FLAG-tagged subdomains of the Man6P/IGF2 receptor. It was determined that 7- 9MycHis is capable of forming a dimeric receptor with all of the FLAG-tagged subdomains.
Binding interactions of the Mannose 6-phosphate/Insulin-like growth factor 2 receptor subdomains
Dr. C.C. and Mabel L. Criss Library
The mannose 6-phosphate/insulin-like growth factor 2 receptor (Man6P/IGF2 receptor) is a mammalian cell membrane receptor involved in the regulation of cellular growth and tumor suppression, making it a necessary component in cancer research studies. The Man6P/IGF2 receptor is composed of several subdomains that are thought to aid in dimerization and proper receptor function. The goal of this research was to determine whether triplet subdomains on each Man6P/IGF2 receptor associate for optimal receptor function, and whether the strength of the interactions between two associating receptors is directly correlated with its molecular-binding abilities. In these studies, we were successful in preparing a MycHis tagged construct of the 7-9 subdomain of the Man6P/IGF2 receptor, confirming protein expression of the construct in cultured mammalian cells, and confirming protein co-expression of 7- 9MycHis with other FLAG-tagged subdomains of the Man6P/IGF2 receptor. It was determined that 7- 9MycHis is capable of forming a dimeric receptor with all of the FLAG-tagged subdomains.