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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2010-11-15
pubmed:abstractText
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 ? as a novel target of S100A6. Importin ? 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 ? in a Ca(2+)-dependent manner, resulting in inhibition of the nuclear localization signal (NLS)-importin ? 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+).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1873-3468
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
19
pubmed:volume
584
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4517-23
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Regulation of nuclear localization signal-importin ? interaction by Ca2+/S100A6.
pubmed:affiliation
Department of Signal Transduction Sciences, Kagawa University, Faculty of Medicine, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't