Linked Life Data

10428833

Source:http://linkedlifedata.com/resource/pubmed/id/10428833

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
1999-9-2
pubmed:databankReference
pubmed:abstractText
We have recently demonstrated that Caenorhabditis elegans Ca(2+)/calmodulin-dependent protein kinase kinase (CeCaM-KK) can activate mammalian CaM-kinase IV in vitro (Tokumitsu, H., Takahashi, N., Eto, K., Yano, S., Soderling, T.R., and Muramatsu, M. (1999) J. Biol. Chem. 274, 15803-15810). In the present study, we have identified and cloned a target CaM-kinase for CaM-KK in C. elegans, CeCaM-kinase I (CeCaM-KI), which has approximately 60% identity to mammalian CaM-KI. CeCaM-KI has 348 amino acid residues with an apparent molecular mass of 40 kDa, which is activated by CeCaM-KK through phosphorylation of Thr(179) in a Ca(2+)/CaM-dependent manner, resulting in a 30-fold decrease in the K(m) of CeCaM-KI for its peptide substrate. Unlike mammalian CaM-KI, CeCaM-KI is mainly localized in the nucleus of transfected cells because the NH(2)-terminal six residues ((2)PLFKRR(7)) contain a functional nuclear localization signal. We have also demonstrated that CeCaM-KK and CeCaM-KI reconstituted a signaling pathway that mediates Ca(2+)-dependent phosphorylation of cAMP response element-binding protein (CREB) and CRE-dependent transcriptional activation in transfected cells, consistent with nuclear localization of CeCaM-KI. These results suggest that the CaM-KK/CaM-KI cascade is conserved in C. elegans and is functionally operated both in vitro and in intact cells, and it may be involved in Ca(2+)-dependent nuclear events such as transcriptional activation through phosphorylation of CREB.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22556-62
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10428833-Amino Acid Sequence, pubmed-meshheading:10428833-Animals, pubmed-meshheading:10428833-Caenorhabditis elegans, pubmed-meshheading:10428833-Calcium-Calmodulin-Dependent Protein Kinase Kinase, pubmed-meshheading:10428833-Calcium-Calmodulin-Dependent Protein Kinase Type 1, pubmed-meshheading:10428833-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:10428833-Cell Compartmentation, pubmed-meshheading:10428833-Cell Nucleus, pubmed-meshheading:10428833-Cloning, Molecular, pubmed-meshheading:10428833-Enzyme Activation, pubmed-meshheading:10428833-Molecular Sequence Data, pubmed-meshheading:10428833-Protein-Serine-Threonine Kinases, pubmed-meshheading:10428833-Sequence Analysis, DNA, pubmed-meshheading:10428833-Sequence Homology, Amino Acid, pubmed-meshheading:10428833-Signal Transduction, pubmed-meshheading:10428833-Species Specificity, pubmed-meshheading:10428833-Transcriptional Activation
pubmed:year
1999
pubmed:articleTitle
Ca(2+)/Calmodulin-dependent protein kinase cascade in Caenorhabditis elegans. Implication in transcriptional activation.
pubmed:affiliation
Helix Research Institute, Inc., 1532-3 Yana, Kisarazu-shi, Chiba 292-0812, Japan.
pubmed:publicationType
Journal Article, Comparative Study