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pubmed-article:15987637pubmed:abstractTextCalmodulin (CaM), a key Ca(2+) sensor in eukaryotes, regulates diverse cellular processes by interacting with many proteins. To identify Ca(2+)/CaM-mediated signaling components, we screened an Arabidopsis expression library with horseradish peroxidase-conjugated Arabidopsis calmodulin2 (AtCaM2) and isolated a homolog of the UBP6 deubiquitinating enzyme family (AtUBP6) containing a Ca(2+)-dependent CaM-binding domain (CaMBD). The CaM-binding activity of the AtUBP6 CaMBD was confirmed by CaM mobility shift assay, phosphodiesterase competition assay and site-directed mutagenesis. Furthermore, expression of AtUBP6 restored canavanine resistance to the Deltaubp6 yeast mutant. This is the first demonstration that Ca(2+) signaling via CaM is involved in ubiquitin-mediated protein degradation and/or stabilization in plants.lld:pubmed
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pubmed-article:15987637pubmed:authorpubmed-author:ChoMoo JeMJlld:pubmed
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pubmed-article:15987637pubmed:articleTitleArabidopsis ubiquitin-specific protease 6 (AtUBP6) interacts with calmodulin.lld:pubmed
pubmed-article:15987637pubmed:affiliationDivision of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju 660-701, Korea.lld:pubmed
pubmed-article:15987637pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15987637pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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