Related Experiment Video

Updated: Dec 26, 2025

Genome-Wide CRISPR Screen for Unveiling Radiosensitive and Radioresistant Genes
08:32

Genome-Wide CRISPR Screen for Unveiling Radiosensitive and Radioresistant Genes

Published on: May 23, 2025

964

The Reduced Oligomerization of MAVS Mediated by ROS Enhances the Cellular Radioresistance

Yarong Du1,2, Dong Pan1, Rong Jia1,3

  • 1Key Laboratory of Space Radiobiology of Gansu Province & CAS Key Laboratory of Heavy Ion Radiation Biology and Medicine, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou 730000, China.

Oxidative Medicine and Cellular Longevity
|March 20, 2020
PubMed

Insights

Mitochondrial antiviral signaling protein (MAVS) suppression enhances radioresistance by protecting against radiation-induced mitochondrial damage and promoting cell survival. This innate immune molecule

Area of Science:

  • Cellular Biology
  • Immunology
  • Radiation Oncology

Background:

  • Mitochondrial antiviral signaling protein (MAVS) is primarily known as an antiviral signaling adaptor.
  • Previous studies suggest MAVS suppression enhances radioresistance, but the underlying mechanisms are unclear.

Purpose of the Study:

  • To elucidate the role of MAVS in cellular response to radiation.
  • To investigate the mechanisms by which MAVS influences radioresistance and mitochondrial function.

Main Methods:

  • Knockdown of MAVS in A549 cells.
  • Assessment of mitochondrial membrane potential and ATP production post-irradiation.
  • Measurement of reactive oxygen species (ROS) generation and proapoptotic protein expression.
  • Inhibition of mitochondrial ROS using MitoQ antioxidant.
  • Analysis of micronucleus (MN) formation and cell survival fraction.

Main Results:

  • MAVS knockdown alleviated radiation-induced mitochondrial dysfunction, reduced ROS generation, and downregulated proapoptotic proteins.
  • Inhibition of mitochondrial ROS with MitoQ decreased MAVS oligomerization and prevented MN formation.
  • MitoQ treatment increased the survival fraction of irradiated A549 cells.

Conclusions:

  • MAVS, an innate immune signaling molecule, plays a role in radiation response.
  • Radiation-induced ROS mediates MAVS oligomerization, contributing to cellular damage.
  • MAVS oligomerization presents a potential therapeutic target for radiotherapy and radioprotection.

More Related Videos

Author Spotlight: Unveiling the Role of TMOD3 in Platinum Resistance and Immune Infiltration in Ovarian Cancer09:40

Author Spotlight: Unveiling the Role of TMOD3 in Platinum Resistance and Immune Infiltration in Ovarian Cancer

Published on: August 2, 2024

3.1K
Identification of Transcription Factor Regulators using Medium-Throughput Screening of Arrayed Libraries and a Dual-Luciferase-Based Reporter11:32

Identification of Transcription Factor Regulators using Medium-Throughput Screening of Arrayed Libraries and a Dual-Luciferase-Based Reporter

Published on: March 27, 2020

7.3K

Related Concept Videos

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...
5.0K
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...
4.5K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.7K
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
6.2K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
5.1K
MicroRNAs01:22

MicroRNAs

MicroRNA (miRNA) are short, regulatory RNA transcribed from introns (non-coding regions of a gene) or intergenic regions (stretches of DNA present between genes). Several processing steps are required to form biologically active, mature miRNA. The initial transcript, called primary miRNA (pri-mRNA), base-pairs with itself, forming a stem-loop structure. Within the nucleus, an endonuclease enzyme, called Drosha, shortens the stem-loop structure into hairpin-shaped pre-miRNA. After the pre-miRNA...
3.6K