EPOP

Last update 08 May 2025

Basic Info

Synonyms

C17orf96, elongin BC and polycomb repressive complex 2 associated protein, Elongin BC and Polycomb repressive complex 2-associated protein

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Introduction

Scaffold protein that serves as a bridging partner between the PRC2/EZH2 complex and the elongin BC complex: required to fine-tune the transcriptional status of Polycomb group (PcG) target genes in embryonic stem cells (ESCs). Plays a key role in genomic regions that display both active and repressive chromatin properties in pluripotent stem cells by sustaining low level expression at PcG target genes: acts by recruiting the elongin BC complex, thereby restricting excessive activity of the PRC2/EZH2 complex. Interaction with USP7 promotes deubiquitination of H2B at promoter sites. Acts as a regulator of neuronal differentiation.

100 Clinical Results associated with EPOP

100 Translational Medicine associated with EPOP

0 Patents (Medical) associated with EPOP

Literatures (Medical) associated with EPOP

01 May 2025·Biochemical and Biophysical Research Communications

Structural analysis of EPOP BC-box binding to the elongin BC complex

Article

Author: Lee, Byung Il ; Yeo, HyunKu ; Kim, Soeun

The elongin BC complex (ELOBC) interacts with BC-box-containing proteins and plays a role in various cellular processes, including transcriptional regulation and ubiquitination. Elongin BC and polycomb repressive complex 2-associated protein (EPOP) contains a BC-box motif in its N-terminal region and influences cancer cell proliferation and differentiation. A previous study showed that a BC-box containing an EPOP-derived peptide suppresses cancer cell growth and induces apoptosis by disrupting the interaction between the ELOBC and its partner proteins. Here, we report the crystal structure of the EPOP BC-box peptide bound to the ELOBC and compare it with the structures of other BC-box-containing proteins in complex with the ELOBC. The overall structure of interactions between the BC-box and the ELOC was similar across different complexes, indicating a conserved binding mode. Our structural analysis revealed that the strictly conserved leucine residue (Leu40) within the BC-box of EPOP, which was previously suggested to be critical for interactions between the BC-box and the ELOC, was deeply embedded in the hydrophobic pocket of the ELOC protein. This study provided structural insights into BC-box-mediated protein-protein interactions and may serve as a fundamental resource for developing small molecules that modulate the interactions between ELOBC and BC-box-containing proteins.

01 Jul 2023·Cell Chemical Biology

Peptide-mediated inhibition of the transcriptional regulator Elongin BC induces apoptosis in cancer cells

Article

Author: Weber, Lisa M ; Trinh, Van Tuan ; Simon, Clara ; Steinchen, Wieland ; Stiewe, Thorsten ; Fischer, Sabrina ; Liefke, Robert ; Forné, Ignasi ; Bange, Gert ; Abendroth, Frank ; Nist, Andrea ; Vázquez, Olalla

Inhibition of protein-protein interactions (PPIs) via designed peptides is an effective strategy to perturb their biological functions. The Elongin BC heterodimer (ELOB/C) binds to a BC-box motif and is essential for cancer cell growth. Here, we report a peptide that mimics the high-affinity BC-box of the PRC2-associated protein EPOP. This peptide tightly binds to the ELOB/C dimer (k_D = 0.46 ± 0.02 nM) and blocks the association of ELOB/C with its interaction partners, both in vitro and in the cellular environment. Cancer cells treated with our peptide inhibitor showed decreased cell viability, increased apoptosis, and perturbed gene expression. Therefore, our work proposes that blocking the BC-box-binding pocket of ELOB/C is a feasible strategy to impair its function and inhibit cancer cell growth. Our peptide inhibitor promises novel mechanistic insights into the biological function of the ELOB/C dimer and offers a starting point for therapeutics linked to ELOB/C dysfunction.

01 Apr 2023·Acta Anaesthesiologica Scandinavica

Unresolved early post‐operative pain trajectory predicts moderate‐to‐severe persistent pain after breast cancer surgery—An observational cohort study

Article

Author: Espitalier, Fabien ; Seegers, Valérie ; Guichoux, Arthur ; Leblanc, Damien ; Sail, Marjorie ; Boré, François

AbstractBackgroundModelling acute post‐operative pain trajectories may improve the prediction of persistent pain after breast cancer surgery (PPBCS). This study aimed to investigate the predictive accuracy of early post‐operative pain (EPOP) trajectories in the development of PPBCS.Materials & MethodsThis observational study was conducted in a French Comprehensive Cancer Centre and included patients who underwent breast cancer surgery from December 2017 to November 2018. Perioperative and follow‐up data were obtained from medical records, and anaesthesia and perioperative charts. EPOP was defined as pain intensity during the first 24 h after surgery, and modelled by a pain trajectory. K‐means clustering method was used to identify patient subgroups with similar EPOP trajectories. The prevalence of moderate‐to‐severe PPBCS (numeric rating scale ≥4) was evaluated until 24 months after surgery.ResultsA total of 608 patients were included in the study, of which 18% (n = 108) and 9% (n = 52) reported mild and moderate‐to‐severe PPBCS, respectively. Based on EPOP trajectories, we were able to identify a low (64%, n = 388), resolved (30%, n = 182), and unresolved (6%, n = 38) pain group. Multivariate analysis identified younger age, axillary lymph node dissection, and unresolved EPOP trajectory as independent risk factors for moderate‐to‐severe PPBCS development. When compared to patients reporting mild PPBCS, moderate‐to‐severe PPBCS patients experienced significantly more neuropathic pain features, pain‐related interference, and delayed opioid cessation.ConclusionEPOP trajectories can distinguish between resolved and unresolved acute pain after breast cancer surgery, allowing early identification of patients at risk to develop significant PPBCS.

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