Related Experiment Video
Updated: Jun 10, 2025
10:25
Using the E1A Minigene Tool to Study mRNA Splicing Changes
Published on: April 22, 2021
4.8K
The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK
Yue-Yu Kong1, Wen-Jie Shu2, Shuang Wang1
1Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, TaiKang Center for Life and Medical Sciences, Frontier Science Center for Immunology and Metabolism, RNA Institute, Wuhan University, Wuhan, 430072, China.
Cell Insight
|October 11, 2024
Summary
The methyltransferase SETD3 enzyme regulates muscle contraction by methylating β-Actin. This study reveals SETD3
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- The methyltransferase SETD3 is known to methylate β-Actin, impacting muscle contraction.
- The broader biological roles of SETD3 beyond actin methylation are not fully understood.
Purpose of the Study:
- To identify novel interacting partners and functions of SETD3.
- To investigate the role of SETD3 in pre-mRNA splicing.
Main Methods:
- In situ proximity labeling coupled with mass spectrometry.
- Genome-wide RNA sequencing.
- Biochemical and bioinformatic analyses.
Main Results:
- SETD3 interacts with numerous splicing factors.
- SETD3 regulates pre-mRNA splicing, particularly exon skipping.
- SETD3 collaborates with hnRNPK to control exon skipping in genes like FNIP1.
Conclusions:
- SETD3 plays a previously unrecognized role in mRNA exon splicing.
- SETD3 and hnRNPK regulate FNIP1 splicing, affecting TFEB nuclear translocation and downstream biogenesis pathways.
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