Ontology highlight
ABSTRACT:
SUBMITTER: Meng D
PROVIDER: S-EPMC2670148 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Meng Dong D Lynch Martin J MJ Huston Elaine E Beyermann Michael M Eichhorst Jenny J Adams David R DR Klussmann Enno E Houslay Miles D MD Baillie George S GS
The Journal of biological chemistry 20090119 17
betaArrestin is a multifunctional signal scaffold protein. Using SPOT immobilized peptide arrays, coupled with scanning alanine substitution and mutagenesis, we show that the MAPK kinase, MEK1, interacts directly with betaarrestin1. Asp(26) and Asp(29) in the N-terminal domain of betaarrestin1 are critical for its binding to MEK1, whereas Arg(47) and Arg(49) in the N-terminal domain of MEK1 are critical for its binding to betaarrestin1. Wild-type FLAG-tagged betaarrestin1 co-immunopurifies with ...[more]