Caspase-6
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.59 caspase-6
Caspase-6 is an executioner caspase, together with caspase-3 (EC 3.4.22.56) and caspase-7 (EC 3.4.22.60), responsible for proteolysis of most cellular polypeptides, e.g. PARP, during apoptosis. Caspase-6 can cleave its own prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61). It has a strict requirement for Asp at P1 and a preferred cleavage sequence Val-Glu-His-Asp-/-. In cells it cleaves lamin A and tau, contributing to nuclear collapse and neurodegeneration. It features a p18/p11 catalytic heterodimer.
Caspase-6 is an executioner caspase, together with caspase-3 (EC 3.4.22.56) and caspase-7 (EC 3.4.22.60), responsible for proteolysis of most cellular polypeptides, e.g. PARP, during apoptosis. Caspase-6 can cleave its own prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61). It has a strict requirement for Asp at P1 and a preferred cleavage sequence Val-Glu-His-Asp-/-. In cells it cleaves lamin A and tau, contributing to nuclear collapse and neurodegeneration. It features a p18/p11 catalytic heterodimer.
References:
Biomedical Dictionary
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