Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-3-22
pubmed:abstractText
The AMP-activated protein kinase (AMPK) is a sensor of cellular energy that is conserved throughout eukaryotes. It is activated by rising AMP, signifying falling energy status caused by starvation for a carbon source or other stress. Binding of AMP to the regulatory gamma subunit triggers phosphorylation of the catalytic alpha subunit by the upstream kinase LKB1, and the activated kinase switches on ATP-generating catabolic pathways while switching off ATP-requiring processes. AMPK inhibits the TOR (target of rapamycin) pathway by phosphorylating TSC2, thus inhibiting cell growth during times of stress. AMPK is also a target for adipokines that regulate energy balance at the whole-body level.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0955-0674
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
167-73
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
New roles for the LKB1-->AMPK pathway.
pubmed:affiliation
Division of Molecular Physiology, Wellcome Trust Biocentre, University of Dundee, Dow Street, Dundee, DD1 4HN, Scotland, UK. d.g.hardie@dundee.ac.uk
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't