METTL3 plays a crucial function in multiple biological processes
Related Experiment Video
Updated: Sep 6, 2025

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
Guilan Li1, Zhanbing Sun1, Weihua Deng1
1Department of Preventive Medicine, School of Public Health, Hengyang Medical School, University of South China, Hengyang, China; Hunan Province Key Laboratory of Typical Environmental Pollution and Health Hazardsa, Hengyang Medical School, University of South China, Hengyang, China.
Abstract:
The N6-methyladenosine (m6A) refers to the methylation of the N6 position of adenosine of RNA adenine. The modification of m6A is one of the most abundant epigenetic modifications in eukaryotic mRNA and non-coding RNA and is controlled by methyltransferases and demethylases. The biological mechanism and significance of m6A have been discovered with the development of m6A sequencing. Various m6A complex components regulate the function of m6A on mRNA. Methyltransferase-like 3 (METTL3) is one of the earliest identified m6A methyltransferases which regulate the functions of m6A. A large number of studies have shown that METTL3 establishes a cross-talk with tumor cells and development of various human diseases. In this review, we will briefly elaborate on the role of METTL3 in biological function, epithelial-mesenchymal transition (EMT), inflammatory response and sensitivity to the resistance of chemo radiotherapies. The underlying molecular mechanism demonstrated by METTL3 may provide a possible target for treating and diagnosing human diseases.
More Related Videos
12:07Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
07:39Cell-Type Specific Protein Purification and Identification from Complex Tissues Using a Mutant Methionine tRNA Synthetase Mouse Line
Published on: April 13, 2022
Related Concept Videos
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Mechanical Protein Functions
Proteins: From Genes to Degradation
Transcription is the synthesis of RNA...
Chemotaxis in E. coli
The Proteasome
MALDI-TOF Mass Spectrometry
Matrix-assisted laser desorption ionization (MALDI) is a commonly...