Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio (Q71824307)

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scientific article published on 01 November 1996

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English	Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio	scientific article published on 01 November 1996

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scholarly article

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21 October 2019

Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio (English)

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21 October 2019

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W A Wilson

1

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21 October 2019

S A Hawley

2

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21 October 2019

D G Hardie

3

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21 October 2019

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1 November 1996

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21 October 2019

Current Biology

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21 October 2019

6

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21 October 2019

11

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21 October 2019

1426-1434

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21 October 2019

Glucose repression in fungi

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Carbon catabolite repression in yeast

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Genetics of carbon catabolite repression in Saccharomyces cerevisiae: genes involved in the derepression process

1 reference

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A yeast gene that is essential for release from glucose repression encodes a protein kinase

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Characterization of tobacco protein kinase NPK5, a homolog of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae

1 reference

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Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA.

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Molecular characterization of yeast regulatory gene CAT3 necessary for glucose derepression and nuclear localization of its product

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Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein

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Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence for physical association of the SNF4 protein with the SNF1 protein kinase

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A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex

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Roles of the Snf1/Rkin1/AMP-activated protein kinase family in the response to environmental and nutritional stress.

1 reference

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Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities

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Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5'-monophosphate.

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5'-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms

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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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Purification of the AMP-activated protein kinase on ATP-gamma-sepharose and analysis of its subunit structure.

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Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase

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Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro

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Catalytic subunits of the porcine and rat 5'-AMP-activated protein kinase are members of the SNF1 protein kinase family

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7 January 2021

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Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I

1 reference

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7 January 2021

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Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase

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Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay

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Active and inactive protein kinases: structural basis for regulation

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Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylase by the AMP-activated protein kinase, demonstrated using freeze-clamping. Effects of high fat diets

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Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast

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Identifiers

10.1016/S0960-9822(96)00747-6

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8939604%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8939604%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

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