BIO230H1 Chapter Notes - Chapter 11: Tnf Receptor Superfamily, Fas Ligand, Apaf1
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BIO230H1 Full Course Notes
Verified Note
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Document Summary
Apoptosis depends on an intracellular proteolytic cascade that is mediated by caspases. They have cysteine at their active site and cleave target proteins at aspartic acid. Initiator (procaspase): ptase domain in tid carboxy terminal region. Apoptotic signal trigger assembly of adaptor protein dimerized and activated. Executioner dimer are activated when cleaved by initiator caspases. Cell-surface death receptors activate the extrinsic pathway of apoptosis. Death receptor: transmembrane protein (tumor necrosis factor receptor family) Fas trimer activation on the target cell surface by fas ligand on the surface of killer lymphocyte bind adaptor with fadd (fas associated death domain)--> initiator. Initiator caspases cleave their partner activate downstream executione -> apoptosis. Binds to adaptor protein apaf1 (apoptotic protease activating factor -1 ), causes apaf1 to oligomerize into apoptosome recruits caspase 9 activate downstream executioner caspase. Each apaf contain a caspases recruitment domain (card), which requires similar. Bcl2 family : regulator of apoptosis pathway.
