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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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FIST/HIPK3: a Fas/ FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activation.

Fas is a cell surface death receptor that signals apoptosis. Several proteins have been identified that bind to the cytoplasmic death domain of Fas. Fas-associated death domain ( FADD), which couples Fas to procaspase-8, and Daxx, which couples Fas to the Jun NH(2)-terminal kinase pathway, bind independently to the Fas death domain. We have identified a 130-kD kinase designated Fas- interacting serine/threonine kinase/homeodomain-interacting protein kinase (FIST/ HIPK3) as a novel Fas-interacting protein. Binding to Fas is mediated by a conserved sequence in the COOH terminus of the protein. FIST/ HIPK3 is widely expressed in mammalian tissues and is localized both in the nucleus and in the cytoplasm. In transfected cell lines, FIST/ HIPK3 causes FADD phosphorylation, thereby promoting FIST/ HIPK3- FADD-Fas interaction. Although Fas ligand- induced activation of Jun NH(2)-terminal kinase is impaired by overexpressed active FIST/ HIPK3, cell death is not affected. These results suggest that Fas- associated FIST/ HIPK3 modulates one of the two major signaling pathways of Fas.[1]

References

  1. FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activation. Rochat-Steiner, V., Becker, K., Micheau, O., Schneider, P., Burns, K., Tschopp, J. J. Exp. Med. (2000) [Pubmed]
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