Latest Paper in FEBS Open Bio

Suppressor of IKKepsilon forms direct interactions with cytoskeletal proteins, tubulin and a-actinin, linking innate immunity to the cytoskeleton

Halie A. Sonnenschein,  Kenneth F. Lawrence, Karli A. Wittenberg, Frank A. Slykas, Emerald L. Dohleman, Jilan B. Knoublauch, Sean M. Fahey, Timothy M. Marshall Jr, James D. Marion, and Jessica K. Bell

Having established that SIKE can be phosphorylated by TBK1 and that innate immune agonists that signal through TLR3 enhance SIKE phosphorylation, the lab is focused on understanding structure-function relationships in SIKE and establishing biological roles of SIKE

Crispr-CAS9 knockout of SIKE shows significantly decreased cell mobility suggesting SIKE may be involved in cytoskeleton rearrangements

 

Structure of SIKE

Biophysical and computational studies of SIKE  suggest it contains intrinsically disordered regions as well as some structure and is largely alpha helical.  SIKE dimerizes and forms higher oligomers