2000 Global Researcher Conference Proceeding
March 10 - 12, 2000
|Conference:||2000 Global Researcher Conference|
|Title:||V2 vasopressin receptor-arrestin interactions|
|Authors:||Innamorati, Giulio; Bowen-Pidgeon, Donna; Sadeghi, Hamid; Birnbaumer, Mariel|
|Institutions:||Vita Salute University School of Medicine, University of Isfahan, National Institute of Environmental Health Sciences, UCLA School of Medicine|
The vasopressin-2 receptor (V2R) is synthesized within the cell and moves to the cell membrane. Exposure of the cell to vasopressin promotes entry of the receptor, a process called internalization. Internalization is aided by a process called phosphorylation, which is a process that links phosphate groups to the tail end of the V2R (i.e. the carboxy terminus). Innamorati, et al., investigated the possible role the cellular substances called non-visual arrestins 2 and 3 had on V2R internalization. They found that the arrestins enhanced V2R internalization and did not interfere with the cell’s ability to keep V2R from once again returning to the cell surface.
The phosphorylated carboxy terminus interacted with the arrestins. However, the researchers found that if a V2R did not have a carboxy terminus, arrestins would still increase the internalization of the V2R. Thus, the research revealed that there are two different sections of the V2R that interact with arrestin to result in increased internalization.