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 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.
Mesh Terms:
14-3-3 Proteins, Amino Acid Sequence, Base Sequence, Calmodulin, Cell Adhesion, DNA Primers, Hela Cells, Humans, Molecular Sequence Data, Protein Binding, Proteins, Recombinant Proteins, Saccharomyces cerevisiae, Signal Transduction, Tyrosine 3-Monooxygenase
14-3-3 Proteins, Amino Acid Sequence, Base Sequence, Calmodulin, Cell Adhesion, DNA Primers, Hela Cells, Humans, Molecular Sequence Data, Protein Binding, Proteins, Recombinant Proteins, Saccharomyces cerevisiae, Signal Transduction, Tyrosine 3-Monooxygenase
J. Cell. Biochem.
Date: Apr. 01, 1999
PubMed ID: 10088721
View in: Pubmed Google Scholar
Download Curated Data For This Publication
1430
Switch View:
- Interactions 2