SRSF3 and HNRNPH1 Regulate Radiation-Induced Alternative Splicing of Protein Arginine Methyltransferase 5 in Hepatocellular Carcinoma

Wen, Chaowei; Tian, Zhujun; Li, Lan; Chen, Tongke; Chen, Huajian; Dai, Jichen; Liang, Zhenzhen; Ma, Shan; Liu, Xiaodong

doi:10.3390/ijms232314832

Cited by 9 publications

(1 citation statement)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Radiotherapy diminishes SRSF3 expression, leading to an elevation in PRMT5-ISO5 levels, which in turn enhances cell radiosensitivity and induces regression of xenograft tumors. 388 NONO, DExH-box helicase 9 (DHX9), and splicing factor proline and glutamine-rich (SFPQ) interact to promote BIN1 exon 12a inclusion. These three proteins are frequently co-expressed in HCC, fostering HCC proliferation, migration, and tumor formation.…”

Section: Colorectal Cancer (Crc)mentioning

confidence: 99%

Alternative splicing and related RNA binding proteins in human health and disease

Tao,

Zhang,

Wang

et al. 2024

Sig Transduct Target Ther

View full text Add to dashboard Cite

Alternative splicing (AS) serves as a pivotal mechanism in transcriptional regulation, engendering transcript diversity, and modifications in protein structure and functionality. Across varying tissues, developmental stages, or under specific conditions, AS gives rise to distinct splice isoforms. This implies that these isoforms possess unique temporal and spatial roles, thereby associating AS with standard biological activities and diseases. Among these, AS-related RNA-binding proteins (RBPs) play an instrumental role in regulating alternative splicing events. Under physiological conditions, the diversity of proteins mediated by AS influences the structure, function, interaction, and localization of proteins, thereby participating in the differentiation and development of an array of tissues and organs. Under pathological conditions, alterations in AS are linked with various diseases, particularly cancer. These changes can lead to modifications in gene splicing patterns, culminating in changes or loss of protein functionality. For instance, in cancer, abnormalities in AS and RBPs may result in aberrant expression of cancer-associated genes, thereby promoting the onset and progression of tumors. AS and RBPs are also associated with numerous neurodegenerative diseases and autoimmune diseases. Consequently, the study of AS across different tissues holds significant value. This review provides a detailed account of the recent advancements in the study of alternative splicing and AS-related RNA-binding proteins in tissue development and diseases, which aids in deepening the understanding of gene expression complexity and offers new insights and methodologies for precision medicine.

show abstract

Section: Colorectal Cancer (Crc)mentioning

confidence: 99%

Alternative splicing and related RNA binding proteins in human health and disease

Tao,

Zhang,

Wang

et al. 2024

Sig Transduct Target Ther

View full text Add to dashboard Cite

show abstract

MACC1 enhances an oncogenic RNA splicing of IRAK1 through interacting with HNRNPH1 in lung adenocarcinoma

Wang,

Li,

Chen

et al. 2024

Journal Cellular Physiology

View full text Add to dashboard Cite

Dysregulation of alternative pre‐mRNA splicing plays a critical role in the progression of cancers, yet the underlying molecular mechanisms remain largely unknown. It is reported that metastasis‐associated in colon cancer 1 (MACC1) is a novel prognostic and predictive marker in many types of cancers, including lung adenocarcinoma. Here, we reveal that the oncogene MACC1 specifically drives the progression of lung adenocarcinoma through its control over cancer‐related splicing events. MACC1 depletion inhibits lung adenocarcinoma progression through triggering IRAK1 from its long isoform, IRAK1‐L, to the shorter isoform, IRAK1‐S. Mechanistically, MACC1 interacts with splicing factor HNRNPH1 to prevent the production of the short isoform of IRAK1 mRNA. Specifically, the interaction between MACC1 and HNRNPH1 relies on the involvement of MACC1's SH3 domain and HNRNPH1's GYR domain. Further, HNRNPH1 can interact with the pre‐mRNA segment (comprising exon 11) of IRAK1, thereby bridging MACC1's regulation of IRAK1 splicing. Our research not only sheds light on the abnormal splicing regulation in cancer but also uncovers a hitherto unknown function of MACC1 in tumor progression, thereby presenting a novel potential therapeutic target for clinical treatment.

show abstract

HNRNPH1 stabilizes FLOT2 mRNA in a non-canonical m6A-dependent manner to promote malignant progression in nasopharyngeal carcinoma

Li,

Liu,

Zeng

et al. 2024

Cell Oncol.

View full text Add to dashboard Cite

SRSF3 and HNRNPH1 Regulate Radiation-Induced Alternative Splicing of Protein Arginine Methyltransferase 5 in Hepatocellular Carcinoma

Cited by 9 publications

References 52 publications

Alternative splicing and related RNA binding proteins in human health and disease

Alternative splicing and related RNA binding proteins in human health and disease

MACC1 enhances an oncogenic RNA splicing of IRAK1 through interacting with HNRNPH1 in lung adenocarcinoma

HNRNPH1 stabilizes FLOT2 mRNA in a non-canonical m6A-dependent manner to promote malignant progression in nasopharyngeal carcinoma

Contact Info

Product

Resources

About