MAPKAPK5, a Novel Mitogen-Activated Protein Kinase (MAPK)-Activated Protein Kinase, Is a Substrate of the Extracellular-Regulated Kinase (ERK) and p38 Kinase
Copyright policy )MAPKAPK5, a Novel Mitogen-Activated Protein Kinase (MAPK)-Activated Protein Kinase, Is a Substrate of the Extracellular-Regulated Kinase (ERK) and p38 Kinase
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 phosphorylated 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.
- University of North Carolina at Chapel Hill United States
- Amgen (United States) United States
Base Sequence, Recombinant Fusion Proteins, Molecular Sequence Data, Intracellular Signaling Peptides and Proteins, JNK Mitogen-Activated Protein Kinases, Sequence Analysis, DNA, Protein Serine-Threonine Kinases, p38 Mitogen-Activated Protein Kinases, Substrate Specificity, Enzyme Activation, Mice, Calcium-Calmodulin-Dependent Protein Kinases, Animals, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Mitogen-Activated Protein Kinases, Phosphorylation, Sequence Alignment
Base Sequence, Recombinant Fusion Proteins, Molecular Sequence Data, Intracellular Signaling Peptides and Proteins, JNK Mitogen-Activated Protein Kinases, Sequence Analysis, DNA, Protein Serine-Threonine Kinases, p38 Mitogen-Activated Protein Kinases, Substrate Specificity, Enzyme Activation, Mice, Calcium-Calmodulin-Dependent Protein Kinases, Animals, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Mitogen-Activated Protein Kinases, Phosphorylation, Sequence Alignment
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