Phosphorylation-independent binding of 14-3-3 to NtCDPK1 by a new mode.
作者： Takeshi Ito , Masaru Nakata , Jutarou Fukazawa , Sarahmi Ishida , Yohsuke Takahashi
DOI: 10.4161/15592324.2014.977721
关键词: Transcription factor 、 Phosphorylation 、 Kinase 、 Cell biology 、 Signal transduction 、 Protein kinase A 、 Biochemistry 、 Scaffold protein 、 Biology 、 Autophosphorylation 、 Plasma protein binding
摘要: 14–3–3 pproteins play essential roles in diverse cellular processes through the direct binding to target proteins. REPRESSION OF SHOOT GROWTH (RSG) is a tobacco (Nicotiana tabacum) transcription factor that involved gibberellin (GA) feedback regulation. The proteins bind RSG depending on phosphorylation of Ser-114 and negatively regulate by sequestering it cytoplasm response GAs. Ca2+-dependent protein kinase NtCDPK1 was identified as an promotes RSG. weakly binds new mode. autophosphorylation necessary for formation between but not its maintenance. In this study, we showed does require when bound NtCDPK1. These data suggest unphosphorylated motif exposed conformational change phosphate group generated
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