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rdf:type |
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lifeskim:mentions |
umls-concept:C0007452,
umls-concept:C0017262,
umls-concept:C0031715,
umls-concept:C0033414,
umls-concept:C0033684,
umls-concept:C0086418,
umls-concept:C0302891,
umls-concept:C1158884,
umls-concept:C1171362,
umls-concept:C1515670,
umls-concept:C2003941,
umls-concept:C2350345,
umls-concept:C2603343
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pubmed:issue |
3
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pubmed:dateCreated |
1996-2-21
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pubmed:abstractText |
Human protein phosphatase-2C alpha (PP2C alpha) was purified to homogeneity after expression in Escherichia coli. AMP inhibited the dephosphorylation of AMP-activated protein kinase (AMPK), but not phosphocasein, by PP2C alpha. The concentration dependence and the effects of other nucleotides (ATP and formycin A-5'-monophosphate) suggest that AMP acts by binding to the same site which causes direct allosteric activation of AMPK. A similar, although less pronounced, effect was observed with another protein phosphatase (PP2AC). We have now shown that AMPK activates the AMPK cascade by four mechanisms, which should make the system exquisitely sensitive to changes in AMP concentration.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AMP-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/PTC1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase 2C
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
377
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
421-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8549768-AMP-Activated Protein Kinases,
pubmed-meshheading:8549768-Adenosine Monophosphate,
pubmed-meshheading:8549768-Allosteric Regulation,
pubmed-meshheading:8549768-Animals,
pubmed-meshheading:8549768-Base Sequence,
pubmed-meshheading:8549768-Cattle,
pubmed-meshheading:8549768-Dose-Response Relationship, Drug,
pubmed-meshheading:8549768-Enzyme Activation,
pubmed-meshheading:8549768-Escherichia coli,
pubmed-meshheading:8549768-Humans,
pubmed-meshheading:8549768-Isoenzymes,
pubmed-meshheading:8549768-Models, Biological,
pubmed-meshheading:8549768-Molecular Sequence Data,
pubmed-meshheading:8549768-Multienzyme Complexes,
pubmed-meshheading:8549768-Nucleotides,
pubmed-meshheading:8549768-Phosphoprotein Phosphatases,
pubmed-meshheading:8549768-Phosphorylation,
pubmed-meshheading:8549768-Protein Kinases,
pubmed-meshheading:8549768-Protein Phosphatase 2,
pubmed-meshheading:8549768-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8549768-Recombinant Proteins,
pubmed-meshheading:8549768-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8549768-Signal Transduction
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pubmed:year |
1995
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pubmed:articleTitle |
5'-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C alpha and native bovine protein phosphatase-2AC.
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pubmed:affiliation |
Department of Biochemistry, The University, Dundee, Scotland, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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