[HTML][HTML] Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a novel MAPK interaction motif
E Åberg, KM Torgersen, B Johansen, SM Keyse… - Journal of biological …, 2009 - ASBMB
ERK3 and ERK4 are atypical MAPKs in which the canonical TXY motif within the activation
loop of the classical MAPKs is replaced by SEG. Both ERK3 and ERK4 bind, translocate,
and activate the MAPK-activated protein kinase (MK) 5. The classical MAPKs ERK1/2 and
p38 interact with downstream MKs (RSK1–3 and MK2–3, respectively) through conserved
clusters of acidic amino acids, which constitute the common docking (CD) domain. In
contrast to the classical MAPKs, the interaction between ERK3/4 and MK5 is strictly …
loop of the classical MAPKs is replaced by SEG. Both ERK3 and ERK4 bind, translocate,
and activate the MAPK-activated protein kinase (MK) 5. The classical MAPKs ERK1/2 and
p38 interact with downstream MKs (RSK1–3 and MK2–3, respectively) through conserved
clusters of acidic amino acids, which constitute the common docking (CD) domain. In
contrast to the classical MAPKs, the interaction between ERK3/4 and MK5 is strictly …