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- W4285992499 abstract "Glucose serves as a universal energy currency in living organisms, however, its potential non-energetic biomolecular functions are less well defined. Glucose was among the most increased analytes among >14,000 assessed across epidermal differentiation, an elevation verified in tissue engineered with fluorescent glucose sensors. Free glucose accumulation, but not its increased metabolism, was essential for epidermal differentiation and required GLUT1, GLUT3, and SGLT1 transporters. Consistent with this, decreasing cellular glucose levels, by restricting available glucose or by increasing intracellular glucose catabolizing enzymes, HK1/2 and G6PD, blocked differentiation and differentiation was also rescued with a non-metabolizable glucose analog. Furthermore, RNA-seq analysis of glucose-depleted epidermal tissue revealed 34% of the genes downregulated by glucose are part of the epidermal differentiation gene signature. ATAC-seq identified candidate transcription factors (TFs) that may act on glucose-regulated genes, including ZNF750, NFE2L2, and IRF6. Glucose affinity chromatography and azido-glucose click chemistry revealed direct glucose binding to a variety of regulatory proteins, including the IRF6 TF whose epidermal knockout confirmed its requirement in glucose-dependent differentiation. Small molecule docking models suggest glucose binds within the DNA binding domain of IRF6. Glucose binding mediated IRF6 dimerization, DNA affinity, and genomic targeting. The IRF6R84C mutant found in poorly differentiated cancers and ectodermal dysplasias was unable to bind glucose. These data demonstrate a non-energetic role for glucose in modulating protein multimerization to control epidermal differentiation." @default.
- W4285992499 created "2022-07-21" @default.
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- W4285992499 date "2022-08-01" @default.
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- W4285992499 title "419 Glucose controls protein-protein interactions and epidermal differentiation" @default.
- W4285992499 doi "https://doi.org/10.1016/j.jid.2022.05.428" @default.
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