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|Title:||The Mitogen-Activated Protein Kinase Scaffold KSR1 is Required for Recruitment of Extracellular Signal-Regulated Kinase to the Immunological Synapse.||Authors:||Giurisato, Emanuele
Lewis, R. E.
Shaw, A. S.
|Keywords:||MAP Kinase; scaffold molecule; immune synapse||Issue Date:||2009||Project:||None||Journal:||MOLECULAR AND CELLULAR BIOLOGY||Abstract:||
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.
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