| First Author | Kilanczyk E | Year | 2011 |
| Journal | Biochem Biophys Res Commun | Volume | 404 |
| Issue | 1 | Pages | 179-83 |
| PubMed ID | 21110948 | Mgi Jnum | J:167451 |
| Mgi Id | MGI:4868305 | Doi | 10.1016/j.bbrc.2010.11.088 |
| Citation | Kilanczyk E, et al. (2011) ERK1/2 is dephosphorylated by a novel phosphatase - CacyBP/SIP. Biochem Biophys Res Commun 404(1):179-83 |
| abstractText | 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+/-3.6mM and 4.3+/-0.4mumol/min, respectively. The CacyBP/SIP phosphatase activity is decreased by okadaic acid (IC(50)=45nM). 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. |
