Advisor Information
Jodi Kreiling
Location
MBSC 201
Presentation Type
Poster
Start Date
6-3-2020 12:30 PM
End Date
6-3-2020 1:45 PM
Abstract
The mannose-6-phosphate/insulin-like growth factor 2 (M6P/IGF2) receptor is a transmembrane protein with the ability to sequester growth factors from the extracellular matrix. This behavior links the receptor to tumor suppression. On a structural level, the extracellular portion of the protein is segmented into 15 homologous repeats, which can be divided further into 5 triplet domains, labelled 1-3, 4-6, 7-9, 10-12, and 13-15. Each triplet receptor displays its own unique ligand binding affinity, including the ability to form dimers with triplets on a second M6P/IGF2 receptor. In fact, previous studies indicate that this protein functions optimally when dimerized. Thus, the purpose of this experiment is to characterize the receptor’s structure and function. Using a urea and dithiothreitol (DTT) disruption assay, the dimerization strength of the receptor’s various domains was assessed. Preliminary results indicate that proximity, and thus, structure, is important in mediating the triplet’s interactions. The 7-9 triplet binds strongly to the same 7-9 triplet on another M6P/IGF2 receptor; however, its association with any other triplet is not as strong comparatively.
Characterization of Dimerization Domains on the Mannose-6-phosphate/Insulin-like Growth Factor 2 Receptor
MBSC 201
The mannose-6-phosphate/insulin-like growth factor 2 (M6P/IGF2) receptor is a transmembrane protein with the ability to sequester growth factors from the extracellular matrix. This behavior links the receptor to tumor suppression. On a structural level, the extracellular portion of the protein is segmented into 15 homologous repeats, which can be divided further into 5 triplet domains, labelled 1-3, 4-6, 7-9, 10-12, and 13-15. Each triplet receptor displays its own unique ligand binding affinity, including the ability to form dimers with triplets on a second M6P/IGF2 receptor. In fact, previous studies indicate that this protein functions optimally when dimerized. Thus, the purpose of this experiment is to characterize the receptor’s structure and function. Using a urea and dithiothreitol (DTT) disruption assay, the dimerization strength of the receptor’s various domains was assessed. Preliminary results indicate that proximity, and thus, structure, is important in mediating the triplet’s interactions. The 7-9 triplet binds strongly to the same 7-9 triplet on another M6P/IGF2 receptor; however, its association with any other triplet is not as strong comparatively.