Proteomics

Dataset Information

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Proteins associated with RORalpha binding element on SULT1E1 gene


ABSTRACT: Estrogen sulfotransferase (SULT1E1) metabolically inactivates estrogen and SULT1E1 expression is tightly regulated by multiple nuclear receptors in cells. A series of biochemical techniques have clearly demonstrated that nuclear receptors HNF4alpha and phosphorylated RORalpha at Ser100 form as complexes binding to the SULT1E1 enhancer to activate gene transcription in response to a high glucose (450 mg/dL) signal. However, the kinase that mediates this phosphorylation at high glucose condition remain in mysterious. To identify these binding factors and possible kinases that mediate the phosphorylation on the SULT1E1 enhancer, the SULT1E1 enhancer was biotinylated and conjugated to magnetic beads, which were subsequently used to enrich the binding factors from low glucose (40 mg/dL) and high glucose (450 mg/dL) treated HepG2 cell nuclear extracts.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte

SUBMITTER: Jason Williams  

LAB HEAD: Jason Williams

PROVIDER: PXD016385 | Pride | 2020-08-26

REPOSITORIES: Pride

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Publications

RORα phosphorylation by casein kinase 1α as glucose signal to regulate estrogen sulfation in human liver cells.

Hu Hao H   Negishi Masahiko M  

The Biochemical journal 20200901 18


Estrogen sulfotransferase (SULT1E1) metabolically inactivates estrogen and SULT1E1 expression is tightly regulated by multiple nuclear receptors. Human fetal, but not adult, livers express appreciable amounts of SULT1E1 protein, which is mimicked in human hepatoma-derived HepG2 cells cultured in high glucose (450 mg/dl) medium. Here, we have investigated this glucose signal that leads to phosphorylation of nuclear receptor RORα (NR1F1) at Ser100 and the transcription mechanism by which phosphory  ...[more]

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