[HTML][HTML] MKP-3, a Novel Cytosolic Protein-tyrosine Phosphatase That Exemplifies a New Class of Mitogen-activated Protein Kinase Phosphatase (∗)
M Muda, U Boschert, R Dickinson, JC Martinou… - Journal of Biological …, 1996 - ASBMB
MKP-1 (also known as CL100, 3CH134, Erp, and hVH-1) exemplifies a class of dual-
specificity phosphatase able to reverse the activation of mitogen-activated protein (MAP)
kinase family members by dephosphorylating critical tyrosine and threonine residues. We
now report the cloning of MKP-3, a novel protein phosphatase that also suppresses MAP
kinase activation state. The deduced amino acid sequence of MKP-3 is 36% identical to
MKP-1 and contains the characteristic extended active-site sequence motif …
specificity phosphatase able to reverse the activation of mitogen-activated protein (MAP)
kinase family members by dephosphorylating critical tyrosine and threonine residues. We
now report the cloning of MKP-3, a novel protein phosphatase that also suppresses MAP
kinase activation state. The deduced amino acid sequence of MKP-3 is 36% identical to
MKP-1 and contains the characteristic extended active-site sequence motif …
