Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 98, Issue 11, Pages 6132-6137Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.111085198
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Caspase-3 is synthesized as a dormant proenzyme and is maintained in an inactive conformation by an Asp-Asp-Asp safety-catch regulatory tripeptide contained within a flexible loop near the large-subunit/smaIl-subunit junction. Removal of this safety catch results in substantially enhanced autocatalytic maturation as well,as increased vulnerability to proteolytic activation by upstream proteases in the apoptotic pathway such as caspase-9 and granzyme B. The safety catch functions through multiple ionic interactions that are disrupted by acidification, which occurs in the cytosol of cells during the early stages of apoptosis. We propose that the caspase-3 safety catch is a key regulatory checkpoint in the apoptotic cascade that regulates terminal events in the caspase cascade by modulating the triggering of caspase-3 activation.
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