The mitogen-activated protein kinase scaffold KSR1 is required for recruitment of extracellular signal-regulated kinase to the immunological synapse

Emanuele Giurisato, Joseph Lin, Angus Harding, Elisa Cerutti, Marina Cella, Robert E. Lewis, Marco Colonna, Andrey S. Shaw

Research output: Contribution to journalArticle

19 Scopus citations


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. Singlecell 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.

Original languageEnglish (US)
Pages (from-to)1554-1564
Number of pages11
JournalMolecular and cellular biology
Issue number6
StatePublished - Mar 1 2009


ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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