Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
45
pubmed:dateCreated
1995-12-26
pubmed:abstractText
AMP-activated protein kinase (AMPK) and Ca2+/calmodulin (CaM)-dependent protein kinase I (CaMKI) are protein kinases that are regulated both by allosteric activation (AMP and Ca2+/CaM, respectively) and by phosphorylation by upstream protein kinases (AMPK kinase (AMPKK) and CaMKI kinase (CaMKIK), respectively). We now report that AMPKK can activate CaMKI and that, conversely, CaMKIK can activate AMPK. CaMKIK is 68-fold more effective at activating CaMKI than AMPK, while AMPKK is 17-fold more effective at activating AMPK than CaMKI. Our results suggest that CaMKIK and AMPKK are distinct enzymes dedicated to their respective kinase targets but with some overlap in their substrate specificities. The availability of alternative substrates for AMPKK and CaMKIK allowed the unequivocal demonstration that AMP and Ca2+/calmodulin promote the activation of AMPK and Ca2+/calmodulin promote the activation of AMPK and CaMKI, respectively, via three independent mechanisms: 1) direct activation of AMPK and CaMKI, 2) activation of AMPKK and CaMKIK, and 3) by binding to AMPK and CaMKI, inducing exposure of their phosphorylation sites. Since AMP and Ca2+/calmodulin each has a triple effect in its respective system, in vivo, the two systems would be expected to be exquisitely sensitive to changes in concentration of their respective activating ligands.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/AMP-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/AMP-activated protein kinase kinase, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent..., http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent..., http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27186-91
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7592975-AMP-Activated Protein Kinases, pubmed-meshheading:7592975-Adenosine Monophosphate, pubmed-meshheading:7592975-Amino Acid Sequence, pubmed-meshheading:7592975-Animals, pubmed-meshheading:7592975-Binding Sites, pubmed-meshheading:7592975-Calcium, pubmed-meshheading:7592975-Calcium-Calmodulin-Dependent Protein Kinase Type 1, pubmed-meshheading:7592975-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:7592975-Calmodulin, pubmed-meshheading:7592975-Enzyme Activation, pubmed-meshheading:7592975-Ligands, pubmed-meshheading:7592975-Molecular Sequence Data, pubmed-meshheading:7592975-Multienzyme Complexes, pubmed-meshheading:7592975-Peptides, pubmed-meshheading:7592975-Phosphorylation, pubmed-meshheading:7592975-Protein Kinases, pubmed-meshheading:7592975-Protein-Serine-Threonine Kinases, pubmed-meshheading:7592975-Substrate Specificity
pubmed:year
1995
pubmed:articleTitle
5'-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms.
pubmed:affiliation
Department of Biochemistry, University, Dundee, Scotland, United Kingdom.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't