Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI.

R. Rose, M. Rose, C. Ottmann

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31 Citations (Scopus)
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Abstract

The regulation and function of peptidylarginine deiminase isoform VI (PAD6), which is a highly abundant protein associated with the cytoplasmic lattices in mammalian oocytes, is poorly understood so far. It has been shown previously, that 14-3-3 proteins, a class of regulatory adapter proteins ubiquitous in eukaryotes, bind to PAD6 in vivo in a phosphorylation dependant manner. Here we identify possible 14-3-3 binding sites in human PAD6 by in silico methods, looking for conserved, surface exposed serine residues. Two of these sites were confirmed as 14-3-3 binding sites by fluorescence polarization competition and X-ray crystallography. We furthermore suggest a role of RSK-type kinases in the phosphorylation of one of these two binding sites and provide evidence in the form of in vitro kinase assays with p70S6 kinase and RSK1
Original languageEnglish
Pages (from-to)65-72
Number of pages8
JournalJournal of Structural Biology
Volume180
DOIs
Publication statusPublished - 2012

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