Importance of extended protease substrate recognition motifs in steering BNIP-2 cleavage by human and mouse granzymes B.

ABSTRACT:

Background

Previous screening of the substrate repertoires and substrate specificity profiles of granzymes resulted in long substrate lists highly likely containing bystander substrates. Here, a recently developed degradomics technology that allows distinguishing efficiently from less efficiently cleaved substrates was applied to study the degradome of mouse granzyme B (mGrB).

Results

In vitro kinetic degradome analysis resulted in the identification of 37 mGrB cleavage events, 9 of which could be assigned as efficiently targeted ones. Previously, cleavage at the IEAD75 tetrapeptide motif of Bid was shown to be efficiently and exclusively targeted by human granzyme B (hGrB) and thus not by mGrB. Strikingly, and despite holding an identical P4-P1 human Bid (hBid) cleavage mot

SUBMITTER: Van Damme P 

PROVIDER: S-EPMC4169252 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature