The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK

The methyltransferase SETD3 is an enzyme essential for catalyzing histidine-73 methylation on β-Actin, thereby promoting its polymerization and regulating muscle contraction. Although increasing evidence suggests that SETD3 is involved in multiple physiological or pathological events, its biological...

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Main Authors: Yue-Yu Kong, Wen-Jie Shu, Shuang Wang, Zhao-Hong Yin, Hongguo Duan, Ke Li, Hai-Ning Du
Format: Article
Language:English
Published: Elsevier 2024-12-01
Series:Cell Insight
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Online Access:http://www.sciencedirect.com/science/article/pii/S2772892724000531
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author Yue-Yu Kong
Wen-Jie Shu
Shuang Wang
Zhao-Hong Yin
Hongguo Duan
Ke Li
Hai-Ning Du
author_facet Yue-Yu Kong
Wen-Jie Shu
Shuang Wang
Zhao-Hong Yin
Hongguo Duan
Ke Li
Hai-Ning Du
author_sort Yue-Yu Kong
collection DOAJ
description The methyltransferase SETD3 is an enzyme essential for catalyzing histidine-73 methylation on β-Actin, thereby promoting its polymerization and regulating muscle contraction. Although increasing evidence suggests that SETD3 is involved in multiple physiological or pathological events, its biological functions remain incompletely understood. In this study, we utilize in situ proximity labeling combined with mass spectrometry analysis to detect potential interacting partners of SETD3. Unexpectedly, we find that many splicing factors are associated with SETD3. Genome-wide RNA sequencing reveals that SETD3 regulates pre-mRNA splicing events, predominantly influencing exon skipping. Biochemical and bioinformatic analyses suggest that SETD3 interacts with hnRNPK, and they collaboratively regulate exon skipping in a common subset of genes. Functionally, we demonstrate that SETD3 and hnRNPK are required for retention of exon 7 skipping in the FNIP1 gene. This promotes FNIP1-mediated nuclear translocation of the transcription factor TFEB and the subsequent induction of lysosomal and mitochondrial biogenesis. Overall, this study uncovers a novel function of SETD3 in modulating mRNA exon splicing.
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institution Kabale University
issn 2772-8927
language English
publishDate 2024-12-01
publisher Elsevier
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series Cell Insight
spelling doaj-art-d3ccfd0169af4e2e8a3b3900c6183d372024-11-10T04:07:53ZengElsevierCell Insight2772-89272024-12-0136100198The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPKYue-Yu Kong0Wen-Jie Shu1Shuang Wang2Zhao-Hong Yin3Hongguo Duan4Ke Li5Hai-Ning Du6Hubei 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, ChinaSchool of Basic Medical Sciences, Xi'an JiaoTong University, Xi'an, 710049, ChinaHubei 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, ChinaHubei 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, ChinaHubei 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, ChinaHubei 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, ChinaHubei 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; Corresponding author.The methyltransferase SETD3 is an enzyme essential for catalyzing histidine-73 methylation on β-Actin, thereby promoting its polymerization and regulating muscle contraction. Although increasing evidence suggests that SETD3 is involved in multiple physiological or pathological events, its biological functions remain incompletely understood. In this study, we utilize in situ proximity labeling combined with mass spectrometry analysis to detect potential interacting partners of SETD3. Unexpectedly, we find that many splicing factors are associated with SETD3. Genome-wide RNA sequencing reveals that SETD3 regulates pre-mRNA splicing events, predominantly influencing exon skipping. Biochemical and bioinformatic analyses suggest that SETD3 interacts with hnRNPK, and they collaboratively regulate exon skipping in a common subset of genes. Functionally, we demonstrate that SETD3 and hnRNPK are required for retention of exon 7 skipping in the FNIP1 gene. This promotes FNIP1-mediated nuclear translocation of the transcription factor TFEB and the subsequent induction of lysosomal and mitochondrial biogenesis. Overall, this study uncovers a novel function of SETD3 in modulating mRNA exon splicing.http://www.sciencedirect.com/science/article/pii/S2772892724000531SETD3RNA splicingRBPshnRNPKFNIP1
spellingShingle Yue-Yu Kong
Wen-Jie Shu
Shuang Wang
Zhao-Hong Yin
Hongguo Duan
Ke Li
Hai-Ning Du
The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK
Cell Insight
SETD3
RNA splicing
RBPs
hnRNPK
FNIP1
title The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK
title_full The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK
title_fullStr The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK
title_full_unstemmed The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK
title_short The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK
title_sort methyltransferase setd3 regulates mrna alternative splicing through interacting with hnrnpk
topic SETD3
RNA splicing
RBPs
hnRNPK
FNIP1
url http://www.sciencedirect.com/science/article/pii/S2772892724000531
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