Counting on mitogen-activated protein kinases—ERKs 3, 4, 5, 6, 7 and 8

• Published in: Cellular Signalling Vol. 16; no. 12; pp. 1345 - 1354
• Main Authors: Bogoyevitch, Marie A., Court, Naomi W.
• Format: Book Review Journal Article
• Language: English
• Published: England Elsevier Inc 01.12.2004
• Subjects: Activation loop sequences; Animals; Extracellular signal regulated protein kinases; Extracellular Signal-Regulated MAP Kinases - physiology; Humans; MAP Kinase Signaling System; MAPK cascades; Mice; Mitogen-Activated Protein Kinase 12 - physiology; Mitogen-Activated Protein Kinase 6 - physiology; Mitogen-Activated Protein Kinase 7 - physiology; Phosphorylation; Signal Transduction; Subcellular localisation; Substrate phosphorylation; Upstream activators; Subcellular localisation; Activation loop sequences; Substrate phosphorylation; MEK/MKK MAPK kinase; JNK; PDZ; Extracellular signal regulated protein kinases; MAPK cascades; MAPK; Upstream activators; ERK; SAPK
• ISSN: 0898-6568; 1873-3913
• DOI: 10.1016/j.cellsig.2004.05.004

Signal transduction pathways in eukaryotic cells integrate diverse extracellular signals, and regulate complex biological responses such as growth, differentiation and death. One group of proline-directed Ser/Thr protein kinases, the mitogen-activated protein kinases (MAPKs), plays a central role in these signalling pathways. Much attention has focused in recent years on three subfamilies of MAPKs, the extracellular signal regulated kinases (ERKs), c-Jun N-terminal kinases (JNKs) and the p38 MAPKs. However, the ERK family is broader than the ERK1 and ERK2 proteins that have been the subject of most studies in this area. Here we overview the work on ERKs 3 to 8, emphasising where possible their biological activities as well as distinctive biochemical properties. It is clear from these studies that these additional ERKs show similarities to ERK1 and ERK2, but with some interesting differences that challenge the paradigm of the archetypical ERK1/2 MAPK pathway.