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

D. Kalabova, A. Smidova, O. Petrvalska, M. Alblova, D. Kosek, P. Man, T. Obsil, V. Obsilova,

. 2017 ; 493 (2) : 940-945. [pub] 20170921

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc18016326

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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$a Petrvalska, Olivia $u Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic; Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, 12843 Prague, Czech Republic.
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$a Alblova, Miroslava $u Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic.
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$a Man, Petr $u BIOCEV-Institute of Microbiology of the Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic.
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$a Obsil, Tomas $u Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic; Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, 12843 Prague, Czech Republic.
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$a Obsilova, Veronika $u Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic. Electronic address: veronika.obsilova@fgu.cas.cz.
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