Fas signalling: Difference between revisions

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&nbsp;Fas is an important cell surface receptor protein that induces apoptosis upon bindin<span id="fck_dom_range_temp_1321447944552_432" />g to the Fas ligand (FasL). This ligand is predominantly expressed in Cytotoxic T-cells and T-Helper Cells.  
&nbsp;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.  
 


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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.
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.

Revision as of 12:57, 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.