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Literature summary for 2.7.11.31 extracted from

  • Chandrashekarappa, D.G.; McCartney, R.R.; ODonnell, A.F.; Schmidt, M.C.
    The beta subunit of yeast AMP-activated protein kinase directs substrate specificity in response to alkaline stress (2016), Cell. Signal., 28, 1881-1893.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.31

Activating Compound

Activating Compound Comment Organism Structure
additional information alkaline and glucose stress leads to the activation of all three isoforms Saccharomyces cerevisiae
additional information alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally HA-tagged or N-terminally triple-FLAG-tagged isozyme in an enzyme-deficient Saccharomyces cerevisiae strain, expression of C-terminally GFP-tagged isozyme in haploid Saccharomyces cerevisiae Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
H379A site-directed mutagenesis, mutation of beta subunit Gal83 with little effect on Gal83 function Saccharomyces cerevisiae
H380A site-directed mutagenesis, mutation of beta subunit Sip2, mutation does not affect heterotrimer association Saccharomyces cerevisiae
H384A site-directed mutagenesis, mutation of beta subunit Gal83 causing a severe loss of function when assayed for growth on alternative carbon sources, the mutation does not affect heterotrimer association Saccharomyces cerevisiae
H772A site-directed mutagenesis, mutation of beta subunit Sip1 does not affect Sip1 function Saccharomyces cerevisiae
additional information point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants Saccharomyces cerevisiae
additional information point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus beta subunit Gal83-containing isozyme after activation by alkaline stress, when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus Saccharomyces cerevisiae 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + Mig1 protein Saccharomyces cerevisiae
-
 ADP + phosphorylated Mig1 protein
-
 ?
ATP + Mig1 protein Saccharomyces cerevisiae S228C
-
 ADP + phosphorylated Mig1 protein
-
 ?
ATP + Mig2 protein Saccharomyces cerevisiae alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2 ADP + phosphorylated Mig2 protein
-
 ?
ATP + Mig2 protein Saccharomyces cerevisiae S228C alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2 ADP + phosphorylated Mig2 protein
-
 ?
additional information Saccharomyces cerevisiae alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2 ?
-
 ?
additional information Saccharomyces cerevisiae S228C alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P32578 beta subunit Sip1, equivalent to subunit beta 1
-
Saccharomyces cerevisiae P34164 beta subunit Sip2, equivalent to subunit beta 2
-
Saccharomyces cerevisiae Q04739 beta subunit Gal83, equivalent to subunit beta 3
-
Saccharomyces cerevisiae S228C P32578 beta subunit Sip1, equivalent to subunit beta 1
-
Saccharomyces cerevisiae S228C P34164 beta subunit Sip2, equivalent to subunit beta 2
-
Saccharomyces cerevisiae S228C Q04739 beta subunit Gal83, equivalent to subunit beta 3
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
additional information cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Mig1 protein
-
 Saccharomyces cerevisiae ADP + phosphorylated Mig1 protein
-
 ?
ATP + Mig1 protein a zinc-finger transcription factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1 Saccharomyces cerevisiae ADP + phosphorylated Mig1 protein
-
 ?
ATP + Mig1 protein a zinc-finger transcriptions factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1 Saccharomyces cerevisiae ADP + phosphorylated Mig1 protein
-
 ?
ATP + Mig1 protein
-
 Saccharomyces cerevisiae S228C ADP + phosphorylated Mig1 protein
-
 ?
ATP + Mig1 protein a zinc-finger transcriptions factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1 Saccharomyces cerevisiae S228C ADP + phosphorylated Mig1 protein
-
 ?
ATP + Mig1 protein a zinc-finger transcription factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1 Saccharomyces cerevisiae S228C ADP + phosphorylated Mig1 protein
-
 ?
ATP + Mig2 protein alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2 Saccharomyces cerevisiae ADP + phosphorylated Mig2 protein
-
 ?
ATP + Mig2 protein a zinc-finger transcriptions factor, the Gal83 isoform is necessary and sufficient for phosphorylation of Mig2 Saccharomyces cerevisiae ADP + phosphorylated Mig2 protein
-
 ?
ATP + Mig2 protein alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2 Saccharomyces cerevisiae S228C ADP + phosphorylated Mig2 protein
-
 ?
ATP + Mig2 protein a zinc-finger transcriptions factor, the Gal83 isoform is necessary and sufficient for phosphorylation of Mig2 Saccharomyces cerevisiae S228C ADP + phosphorylated Mig2 protein
-
 ?
additional information alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2 Saccharomyces cerevisiae ?
-
 ?
additional information alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance Saccharomyces cerevisiae ?
-
 ?
additional information alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance Saccharomyces cerevisiae S228C ?
-
 ?
additional information alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2 Saccharomyces cerevisiae S228C ?
-
 ?

Subunits

Subunits Comment Organism
heterotrimer Snf1 alphabetagamma structure Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
AMP-activated protein kinase
-
 Saccharomyces cerevisiae
AMPK
-
 Saccharomyces cerevisiae
Snf1 kinase
-
 Saccharomyces cerevisiae
SNF1-interacting protein 1
-
 Saccharomyces cerevisiae
SNF1-interacting protein 2
-
 Saccharomyces cerevisiae
SNF1-interacting protein 3
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions Saccharomyces cerevisiae
malfunction deletion of the SAK1 gene blocks nuclear translocation of Gal83 and signaling to Mig2 Saccharomyces cerevisiae
additional information Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions Saccharomyces cerevisiae
physiological function Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress Saccharomyces cerevisiae
physiological function Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress. The nuclear localization of the Gal83 isoform of Snf1 is necessary for its ability to phosphorylate Mig2 Saccharomyces cerevisiae