Establishing a Split Luciferase Assay for Proteinkinase G (PKG) Interaction Studies.

ABSTRACT: Nitric oxide (NO/cyclic guanosine monophosphate (cGMP)-regulated cellular mechanisms are involved in a variety of (patho-) physiological processes. One of the main effector molecules in this system, proteinkinase G (PKG), serves as a molecular switch by phosphorylating different target proteins and thereby turning them on or off. To date, only a few interaction partners of PKG have been described although the identification of protein-protein interactions (PPI) is indispensable for the understanding of cellular processes and diseases. Conventionally used methods to detect PPIs exhibit several disadvantages, e.g., co-immunoprecipitations, which depend on suitable high-affinity antibodies. Therefore, we established a cell-based protein-fragment complementation assay (PCA) for the identificat

SUBMITTER: Schramm A 

PROVIDER: S-EPMC5979328 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature