Regulation of CD95/APO-1/Fas-induced apoptosis by protein phosphatases.
Triggering the CD95/APO-1/Fas receptor by CD95-L induces the assembly of the death-inducing signaling complex (DISC), which permits initiator caspases activation and progression of a signaling cascade that culminates in cellular apoptosis. Despite the CD95 receptor does not exhibit any kinase activity by itself, phosphorylation/dephosphorylation events seem important to regulate many aspects of CD95-mediated apoptosis. Here, we try to highlight particularly the importance of protein phosphatases in the modulation of the CD95 system.
Gloire
Geoffrey
G
GIGA-Research, Unit of Signal Transduction, Laboratory of Virology and Immunology, University of Liège, B-4000 Liège, Belgium.
Charlier
Edith
E
Piette
Jacques
J
D017209:Apoptosis / Q000502:physiology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010766:Phosphorylation; D015398:Signal Transduction; D019014:fas Receptor / Q000502:physiology*
D019014:fas Receptor; D010749:Phosphoprotein Phosphatases