| First Author | Rochat-Steiner V | Year | 2000 |
| Journal | J Exp Med | Volume | 192 |
| Issue | 8 | Pages | 1165-74 |
| PubMed ID | 11034606 | Mgi Jnum | J:65176 |
| Mgi Id | MGI:1913166 | Doi | 10.1084/jem.192.8.1165 |
| Citation | Rochat-Steiner V, et al. (2000) FIST/HIPK3. A Fas/fadd-interacting serine/threonine kinase that induces fadd phosphorylation and inhibits fas-mediated jun nh(2)-terminal kinase activation. J Exp Med 192(8):1165-74 |
| abstractText | 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. |
