Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

UbcH7 interacts with the glucocorticoid receptor and mediates receptor autoregulation.

Garside H, Waters C, Berry A, Rice L, Ardley HC, White A, Robinson PA, Ray D

Unlike other nuclear receptors, transactivation by the glucocorticoid receptor (GR) is increased by the inhibition of the ubiquitin/proteasome pathway. Here, we demonstrate that the ubiquitin-conjugating enzyme (E2), UbcH7, physically interacts with the GR and, when overexpressed, reduces the ability of the receptor to upregulate gene expression. Chemical inhibition of the 26S proteasome abolished the downregulation effect of overexpressed UbcH7, suggesting ... [more]

J. Endocrinol. Sep. 01, 2006; 190(3);621-9 [Pubmed: 17003263]

Throughput

  • Low Throughput

Additional Notes

  • Two-hybrid interaction in the presence of RU486.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
NR3C1 UBE2L3
Affinity Capture-Western
Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
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Curated By

  • BioGRID