Related Experiment Video
Updated: Jun 4, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
17β-estradiol regulates estrogen receptor α monoubiquitination
Piergiorgio La Rosa1, Maria Marino, Filippo Acconcia
1Department of Biology, University Roma Tre, Viale Guglielmo Marconi, 446, Rome, Italy.
Abstract:
Monoubiquitination is a nonproteolytic signal involved in a network of several different physiological processes. Recently, monoubiquitination has been discovered as a new post-transductional modification of the estrogen receptor α (ERα). However, at present no information is available about the role of the cognate ligand 17β-estradiol (E2) in modulating this receptor post-transductional modification. Thus, we studied the E2-dependent modulation of ERα monoubiquitination in different cell lines. Here, we report that ERα monoubiquitination isnegatively modulated by E2. These results demonstrate thatERα monoubiquitination represents a new signalling modification that may modulate the E2:ERα-regulated cellular processes.
Related Concept Videos
Receptor Downregulation in MVBs
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR activation may...
Regulation of Expression at Multiple Steps
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Transducer Mechanism: Nuclear Receptors
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
Regulation of the Unfolded Protein Response

