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In vivo and in vitro association of 14–3‐3 epsilon isoform with calmodulin: Implication for signal transduction and cell proliferation
Author(s) -
Luk Sharon C.W.,
Ngai Saiming,
Tsui Stephen K.W.,
Fung Kwokpui,
Lee Cheukyu,
Waye Mary M.Y.
Publication year - 1999
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19990401)73:1<31::aid-jcb4>3.0.co;2-x
Subject(s) - calmodulin , gene isoform , signal transduction , in vivo , microbiology and biotechnology , in vitro , cell growth , chemistry , biology , biochemistry , genetics , gene , enzyme
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.