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The baculovirus protein p35 inhibits virally induced apoptosis of invertebrate and mammalian cells and may function to impair the clearing of virally infected cells by the host s immune system. This is accomplished at least in part by its ability to block both TNF- and FAS-mediated apoptosis through the inhibition of the ICE family of serine proteases. Two mammalian homologs of baculovirus p35, referred to as inhibitor of apoptosis protein (IAP) 1 and 2, share an amino terminal baculovirus IAP repeat (BIR) motif and a carboxy terminal RING finger. Although the c-IAPs do not directly associate with the TNF receptor (TNF-R), they efficiently block TNF-mediated apoptosis through their interaction with the downstream TNF-R effectors, TRAF1 and TRAF2. Additional IAP family members include ILP (for IAP-like protein) and survivin. ILP inhibits activated caspase-3, leading to the resistance of FAS-mediated apoptosis. Survivin (also designated TIAP) is expressed during the G2/M phase of the cell cycle and associates with microtubules of the mitotic spindle. Increased caspase-3 activity is detected when a disruption of survivin-microtubule interactions occurs.
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