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- W1565365512 abstract "Abstract The enzyme family of heterotrimeric AMP-dependent protein kinases is activated upon low energy states, conferring a switch toward energy-conserving metabolic pathways through immediate kinase actions on enzyme targets and delayed alterations in gene expression through its nuclear relocalization. This family is evolutionarily conserved, including the presence of a ubiquitin-associated (UBA) motif in most catalytic subunits. The potential for the UBA domain to promote protein associations or direct subcellular location, as seen in other UBA-containing proteins, led us to query whether the UBA domain within the yeast AMP-dependent protein kinase ortholog, SNF1 kinase, was important in these aspects of its regulation. Here, we demonstrate that conserved UBA motif mutations significantly alter SNF1 kinase activation and biological activity, including enhanced allosteric subunit associations and increased oxidative stress resistance and life span. Significantly, the enhanced UBA-dependent longevity and oxidative stress response are at least partially dependent on the Fkh1 and Fkh2 stress response transcription factors, which in turn are shown to influence Snf1 gene expression." @default.
- W1565365512 created "2016-06-24" @default.
- W1565365512 creator A5011104850 @default.
- W1565365512 creator A5050783167 @default.
- W1565365512 creator A5054265716 @default.
- W1565365512 creator A5054526401 @default.
- W1565365512 date "2015-06-01" @default.
- W1565365512 modified "2023-10-01" @default.
- W1565365512 title "The SNF1 Kinase Ubiquitin-associated Domain Restrains Its Activation, Activity, and the Yeast Life Span" @default.
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- W1565365512 doi "https://doi.org/10.1074/jbc.m115.647032" @default.
- W1565365512 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4505455" @default.
- W1565365512 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25869125" @default.
- W1565365512 hasPublicationYear "2015" @default.
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