The activity of transcription factors is often modulated by signal responsive protein kinases. Rel/NF-kB transcription factors are regulated by IkB inhibitors, the phosphorylation of which causes ubiquitination and degradation, resulting in nuclear translocation of NFkB and activation of target genes. Here we report pulldown and immunoprecipitation experiments showing that a mammalian 66 kDa protein kinase binds murine c-Rel, both in vitro and in vivo. This kinase appears to have at least two binding sites on c-Rel, a proline-directed serine/ threonine substrate speci®city similar to MAP kinases and to speci®cally phosphorylate the C-terminal domain of murine c-Rel at an ERK consensus site. Oncogene (2000) 19, 2224 ± 2232.
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