Related Experiment Video

Updated: Aug 7, 2025

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

2.6K

RUNX3 Meets the Ubiquitin-Proteasome System in Cancer

Albano Toska1, Nikita Modi1, Lin-Feng Chen1,2

  • 1Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Cells
|March 11, 2023
PubMed

Insights

RUNX3, a transcription factor, acts as a tumor suppressor by degrading oncogenic proteins. However, RUNX3 itself can be degraded via ubiquitination, impacting cancer cell proliferation.

Area of Science:

  • Molecular Biology
  • Cancer Biology
  • Cellular Regulation

Background:

  • RUNX3 is a transcription factor involved in cell proliferation and development.
  • While often a tumor suppressor, RUNX3 can exhibit oncogenic properties in specific cancers.
  • RUNX3 inactivation is common in cancer cells, often mediated by the ubiquitin-proteasome system.

Purpose of the Study:

  • To review the dual role of RUNX3 in cancer.
  • To elucidate mechanisms by which RUNX3 suppresses proliferation via protein degradation.
  • To detail how RUNX3 itself is degraded through ubiquitination.

Main Methods:

  • Literature review of studies on RUNX3 function in cancer.
  • Analysis of ubiquitination and proteasomal degradation pathways.
  • Integration of findings on RNA-, protein-, and pathogen-mediated degradation of RUNX3.

Main Results:

  • RUNX3 suppresses cancer cell proliferation by promoting the ubiquitination and degradation of oncogenic proteins.
  • RUNX3 itself is subject to inactivation through ubiquitination and proteasomal degradation.
  • Various factors, including RNA, proteins, and pathogens, mediate RUNX3 degradation.

Conclusions:

  • RUNX3's function in cancer is context-dependent, involving both tumor suppression and potential oncogenesis.
  • The ubiquitin-proteasome system is critical for regulating RUNX3 levels and activity.
  • Understanding RUNX3 ubiquitination is key to developing targeted cancer therapies.
Keywords:
E3 ligaseRUNX3proteasomal degradationtumor suppressorubiquitination

More Related Videos

Investigation of the Transcriptional Role of a RUNX1 Intronic Silencer by CRISPR/Cas9 Ribonucleoprotein in Acute Myeloid Leukemia Cells09:16

Investigation of the Transcriptional Role of a RUNX1 Intronic Silencer by CRISPR/Cas9 Ribonucleoprotein in Acute Myeloid Leukemia Cells

Published on: September 1, 2019

7.6K
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

10.8K

Related Concept Videos

Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
967
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
924
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
7.4K
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
4.6K
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
3.8K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.9K