Linked Life Data

9661668

Source:http://linkedlifedata.com/resource/pubmed/id/9661668

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-7-27
pubmed:databankReference
pubmed:abstractText
The c-Jun N-terminal kinases (JNKs), also called stress-activated protein kinases (SAPKs), belong to the mitogen-activated protein kinase (MAPK) gene super-family. Like all the MAPKs, JNKs are activated through dual phosphorylation of a theronine residue and a tyrosine residue by a dual specificity kinase such as JNKK1/MKK4/SEK1. Here, we report the molecular cloning and characterization of hJNKK2 alpha, a human homolog of the recently reported murine MKK7 alpha. hJNKK2 alpha belongs to the MAPK kinase gene family and is expressed in many adult tissues. It is nearly identical to a recently reported human JNKK2 at the kinase domain but with major differences in both amino- and carboxyl-terminal sequences, suggesting that hJNKK2 alpha may be an alternative spliced form of this kinase. Expression of hJNKK2 alpha, but not its related kinases JNKK1/MKK4/SEK1, MEK1, MKK3, or MKK6, leads to strong activation of JNK in several cell lines. No activation of ERK or p38 kinases was observed with this kinase. An in-vitro kinase assay demonstrated that JNK1 activation by hJNKK2 alpha requires phosphorylation of the theronine and tyrosine residues at positions 183 and 185 in JNK1. Furthermore, hJNKK2 alpha activated the JNK-dependent signal transduction pathway in vivo by induction of c-Jun- and ATF2-mediated gene transcription. In conclusion, we have cloned the human homolog of murine MKK7 alpha, which may be an alternative spliced form of human JNKK2 involved in transducing specific upstream signals to regulate JNK activity in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
212
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-102
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9661668-Adult, pubmed-meshheading:9661668-Amino Acid Sequence, pubmed-meshheading:9661668-Animals, pubmed-meshheading:9661668-Base Sequence, pubmed-meshheading:9661668-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:9661668-Cloning, Molecular, pubmed-meshheading:9661668-Conserved Sequence, pubmed-meshheading:9661668-DNA, Complementary, pubmed-meshheading:9661668-Enzyme Activation, pubmed-meshheading:9661668-Gene Expression, pubmed-meshheading:9661668-Humans, pubmed-meshheading:9661668-JNK Mitogen-Activated Protein Kinases, pubmed-meshheading:9661668-MAP Kinase Kinase 7, pubmed-meshheading:9661668-Mice, pubmed-meshheading:9661668-Mitogen-Activated Protein Kinase Kinases, pubmed-meshheading:9661668-Mitogen-Activated Protein Kinases, pubmed-meshheading:9661668-Molecular Sequence Data, pubmed-meshheading:9661668-Phosphorylation, pubmed-meshheading:9661668-Protein Kinases, pubmed-meshheading:9661668-Sequence Homology, Amino Acid, pubmed-meshheading:9661668-Signal Transduction
pubmed:year
1998
pubmed:articleTitle
Molecular cloning and characterization of a human protein kinase that specifically activates c-Jun N-terminal kinase.
pubmed:affiliation
Department of Immunology, University of Texas M. D. Anderson Cancer Center, Houston 77030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't