First Author | Kilanczyk E | Year | 2009 |
Journal | Biochem Biophys Res Commun | Volume | 380 |
Issue | 1 | Pages | 54-9 |
PubMed ID | 19166809 | Mgi Jnum | J:144966 |
Mgi Id | MGI:3833026 | Doi | 10.1016/j.bbrc.2009.01.026 |
Citation | Kilanczyk E, et al. (2009) CacyBP/SIP binds ERK1/2 and affects transcriptional activity of Elk-1. Biochem Biophys Res Commun 380(1):54-9 |
abstractText | In this work we showed for the first time that mouse CacyBP/SIP interacts with extracellular signal regulated kinases 1 and 2 (ERK1/2). We also established that a calcium binding protein, S100A6, competes for this interaction. Moreover, the E217K mutant of CacyBP/SIP does not bind significantly to ERK1/2 although it retains the ability to interact with S100A6. Molecular modeling shows that the E217K mutation in the 189-219 CacyBP/SIP fragment markedly changes its electrostatic potential, suggesting that the binding with ERK1/2 might have an electrostatic character. We also demonstrate that CacyBP/SIP-ERK1/2 interaction inhibits phosphorylation of the Elk-1 transcription factor in vitro and in the nuclear fraction of NB2a cells. Altogether, our data suggest that the binding of CacyBP/SIP with ERK1/2 might regulate Elk-1 phosphorylation/transcriptional activity and that S100A6 might further modulate this effect via Ca(2+)-dependent interaction with CacyBP/SIP and competition with ERK1/2. |