In vivo and in vitro association of 14-3-3 epsilon isoform with calmodulin: Implication for signal transduction and cell proliferation

Using a yeast two‐hybrid screen, human 14–3‐3 epsilon protein was found to interact with human calmodulin. In vitro binding assay between human 14–3‐3 epsilon protein/peptide and calmodulin was demonstrated by native gel electrophoresis, and the interaction was shown to be calcium dependent. Our res...

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Veröffentlicht in:Journal of cellular biochemistry 1999-04, Vol.73 (1), p.31-35
Hauptverfasser: Luk, Sharon C.W., Ngai, Sai-ming, Tsui, Stephen K.W., Fung, Kwok-pui, Lee, Cheuk-yu, Waye, Mary M.Y.
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Sprache:eng
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Zusammenfassung:Using a yeast two‐hybrid screen, human 14–3‐3 epsilon protein was found to interact with human calmodulin. In vitro binding assay between human 14–3‐3 epsilon protein/peptide and calmodulin was demonstrated by native gel electrophoresis, and the interaction was shown to be calcium dependent. Our results, along with the association of the 14–3‐3 epsilon protein with other signaling proteins, suggest that the 14–3‐3 protein could provide a link between signal transduction and cell proliferation. J. Cell. Biochem. 73:31–35, 1999. © 1999 Wiley‐Liss, Inc.
ISSN:0730-2312
1097-4644
DOI:10.1002/(SICI)1097-4644(19990401)73:1<31::AID-JCB4>3.0.CO;2-X