Linked Life Data

9822657

Source:http://linkedlifedata.com/resource/pubmed/id/9822657

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
48
pubmed:dateCreated
1998-12-23
pubmed:databankReference
pubmed:abstractText
Ca2+/calmodulin-dependent protein kinases I and IV (CaMKI and CaMKIV, respectively) require phosphorylation on an equivalent single Thr in the activation loop of subdomain VIII for maximal activity. Two distinct CaMKI/IV kinases, CaMKKalpha and CaMKKbeta, were purified from rat brain and partially sequenced (Edelman, A. M., Mitchelhill, K., Selbert, M. A., Anderson, K. A., Hook, S. S., Stapleton, D., Goldstein, E. G., Means, A. R., and Kemp, B. E. (1996) J. Biol. Chem. 271, 10806-10810). We report here the cloning and sequencing of cDNAs for human and rat CaMKKbeta, tissue and regional brain localization of CaMKKbeta protein, and mRNA and functional characterization of recombinant CaMKKbeta in vitro and in Jurkat T cells. The sequences of human and rat CaMKKbeta demonstrate 65% identity and 80% similarity with CaMKKalpha and 30-40% identity with CaMKI and CaMKIV themselves. CaMKKbeta is broadly distributed among rat tissues with highest levels in CaMKIV-expressing tissues such as brain, thymus, spleen, and testis. In brain, CaMKKbeta tracks more closely with CaMKIV than does CaMKKalpha. Bacterially expressed CaMKKbeta undergoes intramolecular autophosphorylation, is regulated by Ca2+/CaM, and phosphorylates CaMKI and CaMKIV on Thr177 and Thr200, respectively. CaMKKbeta activates both CaMKI and CaMKIV when coexpressed in Jurkat T cells as judged by phosphorylated cAMP response element-binding protein-dependent reporter gene expression. CaMKKbeta activity is enhanced by elevation of intracellular Ca2+, although substantial activity is observed at the resting Ca2+ concentration. The strict Ca2+ requirement of CaMKIV-dependent phosphorylation of cAMP response element-binding protein, is therefore controlled at the level of CaMKIV rather than CaMKK.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31880-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:9822657-Amino Acid Sequence, pubmed-meshheading:9822657-Animals, pubmed-meshheading:9822657-Brain, pubmed-meshheading:9822657-Calcium-Calmodulin-Dependent Protein Kinase Kinase, pubmed-meshheading:9822657-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:9822657-Cloning, Molecular, pubmed-meshheading:9822657-DNA, Complementary, pubmed-meshheading:9822657-Enzyme Activation, pubmed-meshheading:9822657-Humans, pubmed-meshheading:9822657-In Situ Hybridization, pubmed-meshheading:9822657-Kinetics, pubmed-meshheading:9822657-Molecular Sequence Data, pubmed-meshheading:9822657-Organ Specificity, pubmed-meshheading:9822657-Phosphorylation, pubmed-meshheading:9822657-Protein-Serine-Threonine Kinases, pubmed-meshheading:9822657-RNA, Messenger, pubmed-meshheading:9822657-Rats, pubmed-meshheading:9822657-Recombinant Proteins, pubmed-meshheading:9822657-Sequence Alignment, pubmed-meshheading:9822657-Sequence Homology, Amino Acid, pubmed-meshheading:9822657-Signal Transduction, pubmed-meshheading:9822657-Transcription, Genetic
pubmed:year
1998
pubmed:articleTitle
Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta.
pubmed:affiliation
Department of Pharmacology and Cancer Biology, Duke University, Durham, North Carolina 27710, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't