| First Author | Francis DM | Year | 2013 |
| Journal | Structure | Volume | 21 |
| Issue | 9 | Pages | 1612-23 |
| PubMed ID | 23932588 | Mgi Jnum | J:245292 |
| Mgi Id | MGI:5916414 | Doi | 10.1016/j.str.2013.07.003 |
| Citation | Francis DM, et al. (2013) The differential regulation of p38alpha by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure 21(9):1612-23 |
| abstractText | The MAP kinase p38alpha is essential for neuronal signaling. To better understand the molecular regulation of p38alpha we used atomistic and molecular techniques to determine the structural basis of p38alpha regulation by the two neuronal tyrosine phosphatases, PTPSL/PTPBR7 (PTPRR) and STEP (PTPN5). We show that, despite the fact that PTPSL and STEP belong to the same family of regulatory proteins, they interact with p38alpha differently and their distinct molecular interactions explain their different catalytic activities. Although the interaction of PTPSL with p38alpha is similar to that of the previously described p38alpha:HePTP (PTPN7) complex, STEP binds and regulates p38alpha in an unexpected manner. Using NMR and small-angle X-ray scattering data, we generated a model of the p38alpha:STEP complex and define molecular differences between its resting and active states. Together, these results provide insights into molecular regulation of p38alpha by key regulatory proteins. |
