ERK1/2 is dephosphorylated by a novel phosphatase--CacyBP/SIP.
Recently, we have reported that the CacyBP/SIP protein binds ERK1/2 (Kilanczyk et al., BBRC, 2009). In this work we show that CacyBP/SIP exhibits a phosphatase activity toward ERK1/2 kinases while its E217K mutant does not. The K(m) and V(max) values established for a standard phosphatase substrate, p-NPP, are 16.9±3.6 mM ... and 4.3±0.4 μmol/min, respectively. The CacyBP/SIP phosphatase activity is decreased by okadaic acid (IC(50)=45 nM). Our experimental results are supported by a theoretical analysis which revealed important sequence similarities between CacyBP/SIP and the phosphatase-like proteins as well as certain MAP kinase phosphatases.
Mesh Terms:
Amino Acid Sequence, Animals, Calcium-Binding Proteins, Cell Line, Tumor, Mice, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Molecular Sequence Data, Phosphoric Monoester Hydrolases, Phosphorylation, Protein Structure, Tertiary
Amino Acid Sequence, Animals, Calcium-Binding Proteins, Cell Line, Tumor, Mice, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Molecular Sequence Data, Phosphoric Monoester Hydrolases, Phosphorylation, Protein Structure, Tertiary
Biochem. Biophys. Res. Commun.
Date: Jan. 07, 2011
PubMed ID: 21110948
View in: Pubmed Google Scholar
Download Curated Data For This Publication
143911
Switch View:
- Interactions 2