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

Citation
Scw. Luk et al., In vivo and in vitro association of 14-3-3 epsilon isoform with calmodulin: Implication for signal transduction and cell proliferation, J CELL BIOC, 73(1), 1999, pp. 31-35
Citations number
31
Categorie Soggetti
Cell & Developmental Biology
Journal title
JOURNAL OF CELLULAR BIOCHEMISTRY
ISSN journal
07302312 → ACNP
Volume
73
Issue
1
Year of publication
1999
Pages
31 - 35
Database
ISI
SICI code
0730-2312(19990401)73:1<31:IVAIVA>2.0.ZU;2-7
Abstract
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 elec trophoresis, and the interaction was shown to be calcium dependent. Our res ults, along with the association of the 14-3-3 epsilon protein with other s ignaling proteins, suggest that the 14-3-3 protein could provide a link bet ween signal transduction and cell proliferation. J. Cell. Biochem. 73:31-35 , 1999. (C) 1999 Wiley-Liss, Inc.