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The c-Fes protein tyrosine kinase is implicated in the differentiation of a number of cell types including neuronal, endothelial and myeloid cells. Structurally, Fes consists of a unique N-terminal region, followed by SH2 (Src homology domain 2) and kinase domains. Two coiled-coil (CC) domains (CC1 and CC2) located within the unique N-terminal region are critical regulators of Fes activity in vivo and may function to recruit Fes activators and/or substrates. A yeast two-hybrid screen, utilizing a K-562 cell cDNA library and the Fes CC2 domain as bait, identified an interacting clone encoding the CC domain and B-box motifs (residues 114-357) of the transcriptional co-repressor KRAB-associated protein (KAP)-1. KAP-1(114-357) interacted with full-length Fes in yeast, and the KAP-1 CC domain was sufficient to bind the Fes N-terminal region in Sf-9 cells. Co-expression of Fes with full-length KAP-1 in human 293T cells stimulated Fes autophosphorylation and led to KAP-1 tyrosine phosphorylation. Association of endogenous Fes and KAP-1 was also observed in HL-60 myeloid leukaemia cells. Together, these data identify a novel Fes-KAP-1 interaction, and suggest a dual role for KAP-1 as both a Fes activator and downstream effector.

The KRAB-associated co-repressor KAP-1 is a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase