Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
28943433
DOI
10.1016/j.bbrc.2017.09.116
PII: S0006-291X(17)31887-9
Knihovny.cz E-zdroje
- Klíčová slova
- 14-3-3, Caspase-2, Phosphorylation, Procaspase-2, Protein-protein interaction,
- MeSH
- fosforylace MeSH
- kaspasa 2 chemie metabolismus MeSH
- lidé MeSH
- proteinové domény MeSH
- proteiny 14-3-3 metabolismus MeSH
- rekombinantní proteiny chemie metabolismus MeSH
- sekvence aminokyselin MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- kaspasa 2 MeSH
- proteiny 14-3-3 MeSH
- rekombinantní proteiny 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.
Citace poskytuje Crossref.org
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