p38 MAP kinases: beyond the stress response
AR Nebreda, A Porras - Trends in biochemical sciences, 2000 - cell.com
Trends in biochemical sciences, 2000•cell.com
Figure 1 p38 mitogen-activated protein kinases (MAPKs) in mammalian cells. The four p38
MAPKs are 60–70% identical in their amino acid sequence. The MAPK kinase MKK6 is a
powerful activator of all p38 isoforms in vitro and it appears to be the major activator of p38
MAPKs in many cell types. MKK3 and MKK4 can also activate certain p38 isoforms. Several
MAPK kinase kinases have been shown to phosphorylate MKK6 in vitro and in co-
transfection experiments, but the physiologically relevant enzymes are still unknown.
MAPKs are 60–70% identical in their amino acid sequence. The MAPK kinase MKK6 is a
powerful activator of all p38 isoforms in vitro and it appears to be the major activator of p38
MAPKs in many cell types. MKK3 and MKK4 can also activate certain p38 isoforms. Several
MAPK kinase kinases have been shown to phosphorylate MKK6 in vitro and in co-
transfection experiments, but the physiologically relevant enzymes are still unknown.
Figure 1 p38 mitogen-activated protein kinases (MAPKs) in mammalian cells. The four p38 MAPKs are 60–70% identical in their amino acid sequence. The MAPK kinase MKK6 is a powerful activator of all p38 isoforms in vitro and it appears to be the major activator of p38 MAPKs in many cell types. MKK3 and MKK4 can also activate certain p38 isoforms. Several MAPK kinase kinases have been shown to phosphorylate MKK6 in vitro and in co-transfection experiments, but the physiologically relevant enzymes are still unknown.
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