rdf:type |
|
lifeskim:mentions |
umls-concept:C0006776,
umls-concept:C0018873,
umls-concept:C0020792,
umls-concept:C0205314,
umls-concept:C0449432,
umls-concept:C0596235,
umls-concept:C0679622,
umls-concept:C1155502,
umls-concept:C1179435,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248,
umls-concept:C1880022
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pubmed:issue |
1-3
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pubmed:dateCreated |
2003-8-25
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pubmed:abstractText |
In this report, we cloned a novel calmodulin-kinase (CaM-KIdelta) from HeLa cells and characterized its activation mechanism. CaM-KIdelta exhibits Ca(2+)/CaM-dependent activity that is enhanced (approximately 30-fold) in vitro by phosphorylation of its Thr180 by CaM-K kinase (CaM-KK)alpha, consistent with detection of CaM-KIdelta-activating activity in HeLa cells. We also identified a novel CaM-KKbeta isoform (CaM-KKbeta-3) in HeLa cells whose activity was highly Ca(2+)/CaM-independent. Transiently expressed CaM-KIdelta exhibited enhanced protein kinase activity in HeLa cells without ionomycin stimulation. This sustained activation of CaM-KIdelta was completely abolished by Thr180Ala mutation and inhibited by CaM-KK inhibitor, STO-609, indicating a functional CaM-KK/CaM-KIdelta cascade in HeLa cells.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Benzimidazoles,
http://linkedlifedata.com/resource/pubmed/chemical/CAMK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Ionomycin,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Isoquinolines,
http://linkedlifedata.com/resource/pubmed/chemical/Naphthalimides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/STO 609,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
|
pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
550
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
57-63
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12935886-Amino Acid Sequence,
pubmed-meshheading:12935886-Animals,
pubmed-meshheading:12935886-Base Sequence,
pubmed-meshheading:12935886-Benzimidazoles,
pubmed-meshheading:12935886-Binding Sites,
pubmed-meshheading:12935886-Calcium-Calmodulin-Dependent Protein Kinase Kinase,
pubmed-meshheading:12935886-Calcium-Calmodulin-Dependent Protein Kinase Type 1,
pubmed-meshheading:12935886-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:12935886-Cloning, Molecular,
pubmed-meshheading:12935886-Enzyme Activation,
pubmed-meshheading:12935886-Enzyme Inhibitors,
pubmed-meshheading:12935886-HeLa Cells,
pubmed-meshheading:12935886-Humans,
pubmed-meshheading:12935886-Ionomycin,
pubmed-meshheading:12935886-Isoenzymes,
pubmed-meshheading:12935886-Isoquinolines,
pubmed-meshheading:12935886-Molecular Sequence Data,
pubmed-meshheading:12935886-Naphthalimides,
pubmed-meshheading:12935886-Phosphorylation,
pubmed-meshheading:12935886-Point Mutation,
pubmed-meshheading:12935886-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12935886-Recombinant Proteins,
pubmed-meshheading:12935886-Sequence Homology, Amino Acid,
pubmed-meshheading:12935886-Signal Transduction,
pubmed-meshheading:12935886-Threonine
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pubmed:year |
2003
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pubmed:articleTitle |
Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells.
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pubmed:affiliation |
Department of Signal Transduction Sciences, Kagawa Medical University, 1750-1 Miki-cho, Kita-gun, Kagawa 761-0793, Japan.
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pubmed:publicationType |
Journal Article
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