Number of the records: 1
Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding
- 1.
SYSNO ASEP 0481658 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding Author(s) Kalábová, Dana (FGU-C) RID, ORCID
Šmídová, Aneta (FGU-C)
Petrvalská, Olivia (FGU-C) RID, ORCID, SAI
Alblová, Miroslava (FGU-C) RID, ORCID
Košek, Dalibor (FGU-C) ORCID, RID
Man, Petr (MBU-M) RID, ORCID
Obšil, Tomáš (FGU-C) RID, ORCID
Obšilová, Veronika (FGU-C) RID, ORCID, SAISource Title Biochemical and Biophysical Research Communications. - : Elsevier - ISSN 0006-291X
Roč. 493, č. 2 (2017), s. 940-945Number of pages 6 s. Language eng - English Country US - United States Keywords procaspase-2 ; 14-3-3 ; protein-protein interaction ; phosphorylation ; caspase-2 Subject RIV EB - Genetics ; Molecular Biology OECD category Biochemistry and molecular biology Subject RIV - cooperation Institute of Microbiology - Biochemistry R&D Projects GA17-00726S GA ČR - Czech Science Foundation (CSF) LQ1604 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Institutional support FGU-C - RVO:67985823 ; MBU-M - RVO:61388971 UT WOS 000413797200011 EID SCOPUS 85029738306 DOI 10.1016/j.bbrc.2017.09.116 Annotation 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. Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2018
Number of the records: 1