Event Title
Cellular Localization of TRPV2 and Molecular Mechanisms of TRPV2 Translocation
Co-investigators
Matthew R. Cohen; Hisashi Fujioka; Mariana Rosca; Charles L. Hoppel; Vera Moiseenkova-Bell (Case Western Reserve University)
Faculty Mentor
Margaret Cochran
Location
Memorial Gym
Start Date
20-4-2012 2:30 PM
End Date
20-4-2012 3:30 PM
Description
Transient receptor potential (TRP) channels perform a diverse range of functions throughout the body. The function of the ubiquitously expressed TRPV2 protein is unknown. Preliminary immunoprecipitation experiments probing for binding partners that may affect TRPV2 trafficking in mouse brain lysate revealed Norbin as a candidate. Co-immunoprecipitation experiments confirmed TRPV2 and Norbin as binding partners under physiological conditions. Immunofluroescence showed that TRPV2 and Norbin co-localize in human neuroblastoma cells. When TRPV2 and Norbin were inserted into an overexpression system, the proteins did not co-immunoprecipitate. This discovery leads to questions about the direct binding capability of Norbin to TRPV2.
Cellular Localization of TRPV2 and Molecular Mechanisms of TRPV2 Translocation
Memorial Gym
Transient receptor potential (TRP) channels perform a diverse range of functions throughout the body. The function of the ubiquitously expressed TRPV2 protein is unknown. Preliminary immunoprecipitation experiments probing for binding partners that may affect TRPV2 trafficking in mouse brain lysate revealed Norbin as a candidate. Co-immunoprecipitation experiments confirmed TRPV2 and Norbin as binding partners under physiological conditions. Immunofluroescence showed that TRPV2 and Norbin co-localize in human neuroblastoma cells. When TRPV2 and Norbin were inserted into an overexpression system, the proteins did not co-immunoprecipitate. This discovery leads to questions about the direct binding capability of Norbin to TRPV2.
Comments
Poster presentation