Linked Life Data

7905477

Source:http://linkedlifedata.com/resource/pubmed/id/7905477

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1994-3-4
pubmed:databankReference
pubmed:abstractText
The AMP-activated protein kinase is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It may also regulate cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. We have purified the AMP-activated protein kinase 14,000-fold from porcine liver. The 63-kDa catalytic subunit co-purifies with two proteins of 40 and 38 kDa that may function as subunits. Partial amino acid sequence of the 63-kDa subunit revealed a striking homology with the catalytic domain of the yeast protein kinase transcriptional regulator Snf1 and its plant homologs. The Snf1 (72 kDa) and Snf4 (36 kDa) complex was also purified and found to phosphorylate the AMP-activated protein kinase peptide substrate, HMRSAMSGLHLVKRR-amide, but was not activated by AMP. Both Snf1/4 and the AMP-activated protein kinase phosphorylate and inactivate yeast acetyl-CoA carboxylase in vitro. These results indicate that during evolution the catalytic domain sequences of the Snf1 protein kinase subfamily have been exploited in the control of mammalian lipid metabolism and raise the possibilities that the AMP-activated protein kinase may have other substrates involved in regulating gene expression pathways, as well as Snf1 homologs participating in the control of lipid metabolism in many eukaryotic organisms.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2361-4
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7905477-AMP-Activated Protein Kinases, pubmed-meshheading:7905477-Acetyl-CoA Carboxylase, pubmed-meshheading:7905477-Amino Acid Sequence, pubmed-meshheading:7905477-Animals, pubmed-meshheading:7905477-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:7905477-Fungal Proteins, pubmed-meshheading:7905477-Liver, pubmed-meshheading:7905477-Macromolecular Substances, pubmed-meshheading:7905477-Molecular Sequence Data, pubmed-meshheading:7905477-Molecular Weight, pubmed-meshheading:7905477-Multienzyme Complexes, pubmed-meshheading:7905477-Phosphorylation, pubmed-meshheading:7905477-Protein Kinases, pubmed-meshheading:7905477-Protein-Serine-Threonine Kinases, pubmed-meshheading:7905477-Rats, pubmed-meshheading:7905477-Saccharomyces cerevisiae, pubmed-meshheading:7905477-Sequence Homology, Amino Acid, pubmed-meshheading:7905477-Substrate Specificity
pubmed:year
1994
pubmed:articleTitle
Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase.
pubmed:affiliation
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't