MEK1 binds directly to betaarrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization.
AuthorsMeng D, Lynch MJ, Huston E, Beyermann M, Eichhorst J, Adams DR, Klussmann E, Klusmann E, Houslay MD, Baillie GS,
JournalJ Biol Chem
PubMed ID19153083
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) ... More