Protein kinase CK1 interacts with and phosphorylates RanBPM in vitro
作者： Uwe Knippschild , Balbina García-Reyes , Joachim Bischof , Sonja Wolff , Doris Henne-Bruns
DOI:
关键词: Scaffold protein 、 Ran 、 Serine 、 Phosphorylation 、 Protein kinase A 、 Biochemistry 、 Chemistry 、 Nuclear transport 、 Casein kinase 1 、 Kinase
摘要: Members of the casein kinase 1 (CK1) family serine/threonine kinases are highly conserved from yeast to mammals and involved in regulation various cellular processes. Specifically, CK1 isoforms δ e have been shown be proliferative processes, differentiation, circadian rhythm, as well nuclear transport. In this report we show that CK1δ interact with murine RanBPM two-hybrid system (YTH) putative CK1δ-interacting domains located between aa 155-386 515-653. Furthermore, mammalian cells partially co-localizes can co-immunoprecipitated RanBPM. addition, strongly phosphorylates within 436-514 vitro . The identification interacting scaffolding protein a new substrate points towards possible function for modulating specific functions.
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