Display Settings:   Send to:  Choose Destination J Biol Chem.
1997 Aug 1;272(31):19509-17.  p38-2, a novel mitogen-activated
protein kinase with distinct properties.   Signal
Pharmaceuticals Inc., San Diego, California 92121, USA.
bstein@signalpharm.com   Mitogen-activated protein (MAP) kinases
are involved in many cellular processes. Here we describe the
cloning and characterization of a new MAP kinase, p38-2. p38-2
belongs to the p38 subfamily of MAP kinases and shares with it
the TGY phosphorylation motif. The complete p38-2 cDNA was
isolated by polymerase chain reaction. It encodes a 364-amino
acid protein with 73% identity to p38. Two shorter isoforms
missing the phosphorylation motif were identified. Analysis of
various tissues demonstrated that p38-2 is differently expressed
from p38. Highest expression levels were found in heart and
skeletal muscle. Like p38, p38-2 is activated by stress-inducing
signals and proinflammatory cytokines. The preferred upstream
kinase is MEK6. Although p38-2 and p38 phosp