Linked Life Data

9878570

Source:http://linkedlifedata.com/resource/pubmed/id/9878570

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-1-20
pubmed:databankReference
pubmed:abstractText
In plants, a number of MAP kinase (MAPK), MAPK kinase (MAPKK), and MAPKK kinase (MAPKKK) homologues have been reported. However, there have been no reports of protein-protein interactions between these kinases or molecular analysis of MAPK cascades in higher plants. To analyze a possible MAPK cascade in Arabidopsis thaliana, we took two molecular approaches. One is the two-hybrid screening of ATMEKK1 (a MAPKKK)-interacting proteins; the other is an analysis of physical and functional interactions among isolated MAPK, MAPKK, and MAPKKK homologues from Arabidopsis. In two-hybrid screening using ATMEKK1 as bait, we isolated a novel MAPKK homologue, ATMKK2, a MAPK homologue, ATMPK4, and an unknown protein. ATMKK2 has high sequence similarity with MEK1 (a MAPKK) in Arabidopsis. Based on yeast two-hybrid analysis, we detected protein-protein interactions between ATMEKK1 and ATMKK2/MEK1 (MAPKKs), between ATMKK2/MEK1 and ATMPK4 (a MAPK), and between ATMPK4 and ATMEKK1. ATMPK4 and ATMKK2/MEK1 interacted with two distinct regions of ATMEKK1, the N-terminal regulatory domain and the C-terminal kinase domain, respectively. Coexpression of ATMEKK1 increased the ability of two closely related MAPKKs, ATMKK2 and MEK1, to complement a growth defect of the yeast pbs2 mutant. Coexpression of ATMPK4 and MEK1 complemented a growth defect of the yeast mpk1 and bck1 mutants. By contrast, other combinations of MAPKs and MAPKKs did not suppress these yeast mutations. These results suggest that ATMEKK1, ATMKK2/MEK1, and ATMPK4 may constitute a MAP kinase cascade.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
532-43
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9878570-Alanine, pubmed-meshheading:9878570-Amino Acid Sequence, pubmed-meshheading:9878570-Amino Acid Substitution, pubmed-meshheading:9878570-Arabidopsis, pubmed-meshheading:9878570-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:9878570-Cloning, Molecular, pubmed-meshheading:9878570-DNA, Complementary, pubmed-meshheading:9878570-Fungal Proteins, pubmed-meshheading:9878570-Genetic Complementation Test, pubmed-meshheading:9878570-MAP Kinase Kinase 2, pubmed-meshheading:9878570-MAP Kinase Kinase Kinases, pubmed-meshheading:9878570-Mitogen-Activated Protein Kinase Kinases, pubmed-meshheading:9878570-Molecular Sequence Data, pubmed-meshheading:9878570-Mutagenesis, Site-Directed, pubmed-meshheading:9878570-Protein Structure, Tertiary, pubmed-meshheading:9878570-Protein-Serine-Threonine Kinases, pubmed-meshheading:9878570-Protein-Tyrosine Kinases, pubmed-meshheading:9878570-Threonine
pubmed:year
1998
pubmed:articleTitle
Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting proteins and analysis of a MAP kinase cascade in Arabidopsis.
pubmed:affiliation
Laboratory of Plant Molecular Biology, Institute of Physical and Chemical Research (RIKEN), Tsukuba Life Science Center, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't