Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8296218 | Biochemical and Biophysical Research Communications | 2017 | 6 Pages |
Abstract
Procaspase-2 phosphorylation at several residues prevents its activation and blocks apoptosis. This process involves procaspase-2 phosphorylation at S164 and its binding to the scaffolding protein 14-3-3. However, bioinformatics analysis has suggested that a second phosphoserine-containing motif may also be required for 14-3-3 binding. In this study, we show that human procaspase-2 interaction with 14-3-3 is governed by phosphorylation at both S139 and S164. Using biochemical and biophysical approaches, we show that doubly phosphorylated procaspase-2 and 14-3-3 form an equimolar complex with a dissociation constant in the nanomolar range. Furthermore, our data indicate that other regions of procaspase-2, in addition to phosphorylation motifs, may be involved in the interaction with 14-3-3.
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Authors
Dana Kalabova, Aneta Smidova, Olivia Petrvalska, Miroslava Alblova, Dalibor Kosek, Petr Man, Tomas Obsil, Veronika Obsilova,