Fas signalling: Difference between revisions
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Fas is an important [[Cell|cell]] surface [[Receptor|receptor]] [[Protein|protein]] that induces apoptosis upon binding to the [[Fas ligand|Fas ligand]] (FasL). This ligand is predominantly expressed in [[Cytotoxic T-cells|Cytotoxic T-cells]] and [[T-Helper Cells|T-Helper Cells]]. | |||
FasL is a trimeric molecule whereas Fas is a monomer, as a consequence the binding of FasL results in the trimerisation of Fas, which the binds death domain-containing adaptor proteins. The adaptor protein recruits and activates [[Caspase 8|Caspase 8]], which in turn cleaves caspase 3. Activated [[Caspase 3|Caspase 3]] then cleaves [[I-CAD|I-CAD]] ( the inhibitor of [[CAD|CAD]]). The final product, CAD (a [[DNAse|DNase]]), is then released into the [[Nucleus|nucleus]] of the cell in order to cleave [[DNA|DNA]]. | |||
FasL is a trimeric molecule whereas Fas is a monomer, as a consequence the binding of FasL results in the trimerisation of Fas, which the binds death domain-containing adaptor proteins. The adaptor protein recruits and activates Caspase 8, which in turn cleaves caspase 3. Activated Caspase 3 then cleaves I-CAD ( the inhibitor of CAD). The final product, CAD (a DNase), is then released into the nucleus of the cell in order to cleave DNA. | |||
Latest revision as of 13:20, 16 November 2011
Fas is an important cell surface receptor protein that induces apoptosis upon binding to the Fas ligand (FasL). This ligand is predominantly expressed in Cytotoxic T-cells and T-Helper Cells.
FasL is a trimeric molecule whereas Fas is a monomer, as a consequence the binding of FasL results in the trimerisation of Fas, which the binds death domain-containing adaptor proteins. The adaptor protein recruits and activates Caspase 8, which in turn cleaves caspase 3. Activated Caspase 3 then cleaves I-CAD ( the inhibitor of CAD). The final product, CAD (a DNase), is then released into the nucleus of the cell in order to cleave DNA.