Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
28943433
DOI
10.1016/j.bbrc.2017.09.116
PII: S0006-291X(17)31887-9
Knihovny.cz E-resources
- Keywords
- 14-3-3, Caspase-2, Phosphorylation, Procaspase-2, Protein-protein interaction,
- MeSH
- Phosphorylation MeSH
- Caspase 2 chemistry metabolism MeSH
- Humans MeSH
- Protein Domains MeSH
- 14-3-3 Proteins metabolism MeSH
- Recombinant Proteins chemistry metabolism MeSH
- Amino Acid Sequence MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Caspase 2 MeSH
- 14-3-3 Proteins MeSH
- Recombinant Proteins MeSH
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.
References provided by Crossref.org
Look for the Scaffold: Multifaceted Regulation of Enzyme Activity by 14-3-3 Proteins
Structural insights into the functional roles of 14-3-3 proteins
