Characterization of an ERK-binding domain in microphthalmia-associated transcription factor and differential inhibition of ERK2-mediated substrate phosphorylation
DM Molina, S Grewal, L Bardwell - Journal of Biological Chemistry, 2005 - ASBMB
Efficient and specific signaling by mitogen-activated protein kinases (MAPKs) is enhanced
by docking sites found on many MAPK substrates and regulators. Here we show that the
MAPKs ERK1 and ERK2 form a stable complex (K d∼ 6 μm) with their substrate the
microphthalmia-associated transcription factor (MITF). Complex formation requires a domain
of MITF of∼ 100 residues that is nearby, but C-terminal to, the MAPK phosphorylation site at
Ser 73. MITF derivatives lacking this ERK-binding domain do not bind ERK2 and are …
by docking sites found on many MAPK substrates and regulators. Here we show that the
MAPKs ERK1 and ERK2 form a stable complex (K d∼ 6 μm) with their substrate the
microphthalmia-associated transcription factor (MITF). Complex formation requires a domain
of MITF of∼ 100 residues that is nearby, but C-terminal to, the MAPK phosphorylation site at
Ser 73. MITF derivatives lacking this ERK-binding domain do not bind ERK2 and are …
