| First Author | Ni H | Year | 1998 |
| Journal | Biochem Biophys Res Commun | Volume | 243 |
| Issue | 2 | Pages | 492-6 |
| PubMed ID | 9480836 | Mgi Jnum | J:45995 |
| Mgi Id | MGI:1196798 | Doi | 10.1006/bbrc.1998.8135 |
| Citation | Ni H, et al. (1998) MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase. Biochem Biophys Res Commun 243(2):492-6 |
| abstractText | A novel protein kinase that has significant sequence homology to mitogen-activated protein kinase (MAPK)-activated protein kinase (MAPKAPK) was identified. This novel protein kinase has a nucleotide sequence that encodes a protein of 473 amino acids and shares 45%, 46%, and 44% amino acid sequence identities to MAPKAPK2, 3 and 4 respectively. Northern blot analysis revealed that it has a wide tissue distribution. This novel protein kinase designated MAPKAPK5 can be phospho-rylated by extracellular-regulated kinase (ERK), and p38 kinase but not by c-jun N-terminal kinase (JNK) in vitro. Recombinant GST- MAPKAPK5 protein can phosphorylate a peptide derived from the regulatory light chain of myosin II. Phosphorylation of MAPKAPK5 by ERK and p38 kinase increased its activity by 9 and 15 fold respectively. Taken together, these data suggest that MAPKAPK5 is a novel in vitro substrate for ERK and p38 kinase. |
