Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding

Kalábová, Dana; Šmídová, Aneta; Petrvalská, Olivia; Alblová, Miroslava; Košek, Dalibor; Man, Petr; Obšil, Tomáš; Obšilová, Veronika

doi:https://dx.doi.org/10.1016/j.bbrc.2017.09.116

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, SAI}
Source Title	Biochemical and Biophysical Research Communications. - : Elsevier - ISSN 0006-291X Roč. 493, č. 2 (2017), s. 940-945
Number 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