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Regulation of nuclear localization signal-importin α interaction by Ca2+/S100A6.
- Source :
-
FEBS letters [FEBS Lett] 2010 Nov 19; Vol. 584 (22), pp. 4517-23. Date of Electronic Publication: 2010 Oct 21. - Publication Year :
- 2010
-
Abstract
- Although the precise intracellular roles of S100 proteins are not fully understood, these proteins are thought to be involved in Ca(2+)-dependent diverse signal transduction pathways. In this report, we identified importin α as a novel target of S100A6. Importin α contains armadillo repeats, essential for binding to nuclear localization signals. Based on the results from GST pull-down assay, gel-shift assay, and co-immunoprecipitation, we demonstrated that S100A6 specifically interacts with the armadillo repeats of importin α in a Ca(2+)-dependent manner, resulting in inhibition of the nuclear localization signal (NLS)-importin α complex formation in vitro and in vivo. These results indicate S100A6 may regulate the nuclear transport of NLS-cargos in response to increasing concentrations of intracellular Ca(2+).<br /> (Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Binding Sites
COS Cells
Chlorocebus aethiops
Humans
Molecular Sequence Data
Mutation
Nuclear Localization Signals chemistry
Protein Binding
Protein Structure, Tertiary
Simian virus 40
alpha Karyopherins chemistry
alpha Karyopherins genetics
beta Karyopherins metabolism
Calcium metabolism
Nuclear Localization Signals metabolism
S100 Proteins metabolism
alpha Karyopherins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 584
- Issue :
- 22
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 20965181
- Full Text :
- https://doi.org/10.1016/j.febslet.2010.09.052