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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2005-7-15
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pubmed:abstractText |
Calmodulin (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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CALM2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Canavanine,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Horseradish Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/ubiquitin-specific protease
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author |
pubmed-author:CheongMi SunMS,
pubmed-author:ChoMoo JeMJ,
pubmed-author:ChoiMan SooMS,
pubmed-author:ChungWoo SikWS,
pubmed-author:KangYun HwanYH,
pubmed-author:KimMin ChulMC,
pubmed-author:KooSung CheolSC,
pubmed-author:LeeSang MinSM,
pubmed-author:LimChae OhCO,
pubmed-author:MoonByeong CheolBC,
pubmed-author:ParkChan YoungCY,
pubmed-author:YooJae HyukJH
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
579
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3885-90
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15987637-Amino Acid Motifs,
pubmed-meshheading:15987637-Amino Acid Sequence,
pubmed-meshheading:15987637-Arabidopsis,
pubmed-meshheading:15987637-Arabidopsis Proteins,
pubmed-meshheading:15987637-Binding, Competitive,
pubmed-meshheading:15987637-Calcium,
pubmed-meshheading:15987637-Calmodulin,
pubmed-meshheading:15987637-Canavanine,
pubmed-meshheading:15987637-Dose-Response Relationship, Drug,
pubmed-meshheading:15987637-Endopeptidases,
pubmed-meshheading:15987637-Gene Library,
pubmed-meshheading:15987637-Genetic Complementation Test,
pubmed-meshheading:15987637-Glutathione Transferase,
pubmed-meshheading:15987637-Horseradish Peroxidase,
pubmed-meshheading:15987637-Humans,
pubmed-meshheading:15987637-Models, Genetic,
pubmed-meshheading:15987637-Molecular Sequence Data,
pubmed-meshheading:15987637-Mutagenesis, Site-Directed,
pubmed-meshheading:15987637-Mutation,
pubmed-meshheading:15987637-Peptides,
pubmed-meshheading:15987637-Phosphoric Diester Hydrolases,
pubmed-meshheading:15987637-Protein Binding,
pubmed-meshheading:15987637-Protein Structure, Tertiary,
pubmed-meshheading:15987637-Sequence Homology, Amino Acid,
pubmed-meshheading:15987637-Signal Transduction,
pubmed-meshheading:15987637-Ubiquitin
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pubmed:year |
2005
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pubmed:articleTitle |
Arabidopsis ubiquitin-specific protease 6 (AtUBP6) interacts with calmodulin.
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pubmed:affiliation |
Division of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju 660-701, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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