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Engineered hybrid dimers: tracking the activation pathway of caspase-7.

Abstract：

:Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis within a region that separates the large and small chains of each domain. Using hybrid dimers we distinguish the relative contribution of each domain to catalysis by the whole molecule. We demonstrate that the zymogen arises from direct dimerization and not domain swapping. In contrast to previous conclusions, we show that only one of the catalytic domains must be proteolyzed to enable activation. The processed domain of this singly cleaved zymogen has the same catalytic activity as a domain of fully active caspase-7. A transient intermediate of singly cleaved dimeric caspase-7 can be found in a cell-free model of apoptosis induction. However, we see no evidence for an analogous intermediate of the related executioner caspase-3. Our study demonstrates the efficiency by which the executioner caspases are activated in vivo.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Denault JB,Békés M,Scott FL,Sexton KM,Bogyo M,Salvesen GS

doi

10.1016/j.molcel.2006.06.020

subject

Has Abstract

pub_date

2006-08-01 00:00:00

pages

523-33

issue

4

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(06)00444-8

journal_volume

23

pub_type

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