Caspase-3 Regulatory Mechanisms: Difference between revisions
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Aside from phosphorylation, caspase-3 is also known to be ubiquitinylated and nitrosylated, however the underlying mechanismsand effect of these modifications are still unclear. | Aside from phosphorylation, caspase-3 is also known to be ubiquitinylated and nitrosylated, however the underlying mechanismsand effect of these modifications are still unclear. | ||
=== Natural Inhibitors=== | |||
<scene name='Caspase-3_Regulatory_Mechanisms/Bir2/1'>Casp3 bound to BIR2 domain</scene> | <scene name='Caspase-3_Regulatory_Mechanisms/Bir2/1'>Casp3 bound to BIR2 domain</scene> | ||
X-linked inhibitor of apoptosis proteins (XIAP) contains the second baculovirus IAP repeat domain (BIR2) targeting caspase-3 and caspase-7. The <scene name='Caspase-3_Regulatory_Mechanisms/Bir2/2'>BIR2</scene> domain sits directly in the active site of caspase-3 and completely inhibits the protein. The region binding the active site runs in the opposite direction of normal caspase-3 substrates, thus occupying P1 through P4 but avoiding cleavage by the protease. This unique method of inhibition is a critical regulatory mechanism used in cells to control apoptotic caspase activity. | X-linked inhibitor of apoptosis proteins (XIAP) contains the second baculovirus IAP repeat domain (BIR2) targeting caspase-3 and caspase-7. The <scene name='Caspase-3_Regulatory_Mechanisms/Bir2/2'>BIR2</scene> domain sits directly in the active site of caspase-3 and completely inhibits the protein. The region binding the active site runs in the opposite direction of normal caspase-3 substrates, thus occupying P1 through P4 but avoiding cleavage by the protease. This unique method of inhibition is a critical regulatory mechanism used in cells to control apoptotic caspase activity. | ||
= | =References= | ||
Bose, K., C. Pop, et al. (2003). "An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3." Biochemistry 42(42): 12298-12310. | Bose, K., C. Pop, et al. (2003). "An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3." Biochemistry 42(42): 12298-12310. | ||