Source:http://linkedlifedata.com/resource/pubmed/id/10417704
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1999-12-9
|
pubmed:databankReference | |
pubmed:abstractText |
AKINalpha1, a Ser/Thr kinase from Arabidopsis thaliana belongs to the highly conserved SNF1 family of protein kinases in eukaryotes. Recent data suggest that the plant SNF1-related kinases (SnRK1 family) are key enzymes implicated in the regulation of carbohydrate and lipid metabolism. In Saccharomyces cerevisiae and mammals, the SNF1 and AMPKalpha protein kinases interact with two other families of proteins, namely SNF4/AMPKgamma and SIP1/SIP2/GAL83/AMPKbeta, to form active heterotrimeric complexes. In this paper, we describe the characterisation of three novel cDNAs. AKINbeta1 and AKINbeta2 encode proteins similar to SIP1, SIP2 and GAL83 and AKINgamma codes for a protein showing similarity with SNF4. Using the two-hybrid system, specific interactions have been shown between A. thaliana AKINbeta1/beta2, AKINgamma and AKINgamma as well as between the A. thaliana and S. cerevisiae subunits. Interestingly, AKINbeta1, AKINbeta2 and AKINgamma mRNAs accumulate differentially in A. thaliana tissues and are modulated during development and under different growth conditions. These data suggest the presence in higher plants of a conserved heterotrimeric complex. Moreover, the differential transcription of different non-catalytic subunits can constitute a first level of regulation of the SNF1-like complex in plants.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/SNF1-related protein kinases
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0960-7412
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
18
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
541-50
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10417704-Amino Acid Sequence,
pubmed-meshheading:10417704-Arabidopsis,
pubmed-meshheading:10417704-DNA, Complementary,
pubmed-meshheading:10417704-Genes, Plant,
pubmed-meshheading:10417704-Light,
pubmed-meshheading:10417704-Molecular Sequence Data,
pubmed-meshheading:10417704-Plant Proteins,
pubmed-meshheading:10417704-Protein Binding,
pubmed-meshheading:10417704-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10417704-RNA, Messenger,
pubmed-meshheading:10417704-RNA, Plant,
pubmed-meshheading:10417704-Sequence Homology, Amino Acid,
pubmed-meshheading:10417704-Signal Transduction,
pubmed-meshheading:10417704-Tissue Distribution
|
pubmed:year |
1999
|
pubmed:articleTitle |
Arabidopsis thaliana proteins related to the yeast SIP and SNF4 interact with AKINalpha1, an SNF1-like protein kinase.
|
pubmed:affiliation |
Laboratoire de Biologie du Dveloppement des Plantes, Institut de Biotechnologie des Plantes, UMR CNRS 8618, Université de Paris-Sud, Orsay, France.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|