| First Author | Giurisato E | Year | 2009 |
| Journal | Mol Cell Biol | Volume | 29 |
| Issue | 6 | Pages | 1554-64 |
| PubMed ID | 19139278 | Mgi Jnum | J:145865 |
| Mgi Id | MGI:3836213 | Doi | 10.1128/MCB.01421-08 |
| Citation | Giurisato E, et al. (2009) The mitogen-activated protein kinase scaffold KSR1 is required for recruitment of extracellular signal-regulated kinase to the immunological synapse. Mol Cell Biol 29(6):1554-64 |
| abstractText | KSR1 is a mitogen-activated protein (MAP) kinase scaffold that enhances the activation of the MAP kinase extracellular signal-regulated kinase (ERK). The function of KSR1 in NK cell function is not known. Here we show that KSR1 is required for efficient NK-mediated cytolysis and polarization of cytolytic granules. Single-cell analysis showed that ERK is activated in an all-or-none fashion in both wild-type and KSR1-deficient cells. In the absence of KSR1, however, the efficiency of ERK activation is attenuated. Imaging studies showed that KSR1 is recruited to the immunological synapse during T-cell activation and that membrane recruitment of KSR1 is required for recruitment of active ERK to the synapse. |
