Abstract：
:In the death receptor induced apoptotic pathway, caspase-8 autocatalytically cleaves itself at specific cleavage sites. To better understand the regulatory mechanisms behind caspase-8 activation, we compared active wild-type caspase-8 (wtC8) and an uncleavable form of procaspase-8 (uncleavable C8). We demonstrate that wtC8 predominantly exists as a monomer and dimerizes in a concentration and inhibitor binding-dependent fashion. The K(D) for dimeric wtC8 is approximately 50 micro M and decreases when inhibitor bound. Uncleavable C8 is mainly monomeric, but a small amount that dimerizes is as active as wtC8. Inhibitor binding does not favor dimerization but induces active site rearrangements in uncleavable C8. Our findings suggest that dimerization is the crucial factor for caspase-8 activation.
journal_name
Mol Celljournal_title
Molecular cellauthors
Donepudi M,Mac Sweeney A,Briand C,Grütter MGdoi
10.1016/s1097-2765(03)00059-5subject
Has Abstractpub_date
2003-02-01 00:00:00pages
543-9issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(03)00059-5journal_volume
11pub_type
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