Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2003-8-25
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
550
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-63
pubmed:dateRevised
2007-11-15
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
pubmed:year
2003
pubmed:articleTitle
Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells.
pubmed:affiliation
Department of Signal Transduction Sciences, Kagawa Medical University, 1750-1 Miki-cho, Kita-gun, Kagawa 761-0793, Japan.
pubmed:publicationType
Journal Article