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


Autoria(s): Rochat-Steiner V.; Becker K.; Micheau O.; Schneider P.; Burns K.; Tschopp J.
Data(s)

2000

Resumo

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.

Identificador

https://serval.unil.ch/?id=serval:BIB_629A98B92559

isbn:0022-1007 (Print)

pmid:11034606

doi:10.1084/jem.192.8.1165

isiid:000089983900010

http://my.unil.ch/serval/document/BIB_629A98B92559.pdf

http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_629A98B925596

Idioma(s)

en

Direitos

info:eu-repo/semantics/openAccess

Fonte

Journal of Experimental Medicine, vol. 192, no. 8, pp. 1165-1174

Palavras-Chave #Adaptor Proteins, Signal Transducing; Animals; Antigens, CD95/metabolism; Apoptosis; Carrier Proteins/genetics; Carrier Proteins/metabolism; Cloning, Molecular; Fas-Associated Death Domain Protein; Female; Gene Library; Humans; Intracellular Signaling Peptides and Proteins; JNK Mitogen-Activated Protein Kinases; Jurkat Cells; Male; Mice; Mitogen-Activated Protein Kinases/antagonists & inhibitors; Mitogen-Activated Protein Kinases/metabolism; Organ Specificity; Phosphorylation; Protein-Serine-Threonine Kinases/genetics; Protein-Serine-Threonine Kinases/metabolism; Recombinant Proteins/metabolism; Saccharomyces cerevisiae Proteins; Transcription, Genetic; Tumor Cells, Cultured
Tipo

info:eu-repo/semantics/article

article