Emerging roles of hnRNP A2B1 in cancer and inflammation

Xu, Huangru; Li, Ping; Wang, Xiaoyang; Zhuang, Hongqin; Zhang, Hua

doi:10.1016/j.ijbiomac.2022.09.104

Cited by 10 publications

(6 citation statements)

References 191 publications

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“…The significance of the hnRNP family has been gradually discovered in a variety of cancers (Howley et al, 2022; Y. Li et al, 2021; Xu et al, 2022). However, to date, only a few reports exist in the literature about HNRNPR in tumors.…”

Section: Discussionmentioning

confidence: 99%

Pan‐cancer analysis of the oncogenic role of HNRNPR in human tumors

Yang

Sun

Xiang

2023

Cell Biology International

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Heterogeneous nuclear ribonucleoproteins (hnRNPs) are potential cancer biomarkers. Little is known about the role of HNRNPR, an essential member of the hnRNP family, in human tumours. This study aims to explore the potential value of HNRNPR across cancers, based on The Cancer Genome Atlas (TCGA). The expression level, mutation, DNA methylation, phosphorylation status, survival status, pathological stage, tumor mutation burden (TMB), microsatellite instability (MSI), immune cell infiltration, and immune signature related to HNRNPR were analyzed. HNRNPR expression level was increased in several types of cancer and was associated with poor prognosis, especially in liver hepatocellular carcinoma (LIHC). HNRNPR was also correlated with antitumour immunity, and associated with TMB, MSI, and immune cell activation status across cancers. Furthermore, nomograms were established to predict the prognosis of LIHC, based on HNRNPR and other clinical characteristics. Functional enrichment analysis showed the mechanisms of HNRNPR‐mediated LIHC progression. Loss‐of‐function experiments demonstrated that inhibition of HNRNPR could remarkably suppress hepatocellular carcinoma (HCC) cell proliferation, migration, invasion, and Epithelial‐Mesenchymal Transition abilities. Our study offers a comprehensive understanding of the oncogenic roles of HNRNPR across different tumours, and demonstrates that HNRNPR might foster the proliferation, migration, and invasion abilities of HCC cells.

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Section: Discussionmentioning

confidence: 99%

Pan‐cancer analysis of the oncogenic role of HNRNPR in human tumors

Yang

Sun

Xiang

2023

Cell Biology International

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“…HnRNPs can bind to m6A in pre-miRNAs and can also regulate the processing of pre-miRNAs. 33 YTHDC1 can regulate mRNA splicing and mRNA transportation to the cytoplasm. 34 As mRNA with m6A modification enters the cytoplasm, YTHDF1, YTHDF3, and YTHDC2 can recognize this modification and promote mRNA translation.…”

Section: F I G U R E 1 (See Caption On Next Page)mentioning

confidence: 99%

“…Among them, hnRNP A2B1 can directly bind to m6A‐modified pri‐miRNA and promote the processing of pri‐miRNA together with other proteins (Figure 2B). HnRNPs can bind to m6A in pre‐miRNAs and can also regulate the processing of pre‐miRNAs 33 . YTHDC1 can regulate mRNA splicing and mRNA transportation to the cytoplasm 34 .…”

Section: Writers Readers and Erasers Of M6a Modificationmentioning

confidence: 99%

Roles of rRNA N‐methyladenosine modification in the function of ribosomes

Yang,

Wang,

Huang

et al. 2023

Cell Biochemistry & Function

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The N‐methyladenosine (m6A) modification of ribosomal RNA (rRNA) plays critical roles in regulating the function of ribosomes, the essential molecular machines that translate genetic information from mRNA into proteins. Specifically, m6A modification affects ribosome biogenesis, stability, and function by regulating the processing and maturation of rRNA, the assembly and composition of ribosomes, and the accuracy and efficiency of translation. Furthermore, m6A modification allows for dynamic regulation of translation in response to environmental and cellular signals. Therefore, a deeper understanding of the mechanisms and functions of m6A modification in rRNA will advance our knowledge of ribosome‐mediated gene expression and facilitate the development of new therapeutic strategies for ribosome‐related diseases.

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“…hnRNPA2/B1 primarily resides in the nucleus, and trafficking of hnRNPA2/B1 to the cytoplasm is mediated by nuclear localization signals in the GRD . In medical research, the importance of hnRNPA2/B1 is significant as many diseases are associated with hnRNPA2/B1, for instance, breast, lung, liver, and pancreatic cancers, neurodegenerative diseases, such as Alzheimer’s disease, ataxia syndrome, and autoimmune diseases. , Hence, drug discovery that targets hnRNPA2/B1 could represent a novel strategy as overexpression of the hnRNPA2/B1 has been manifested in cancer . Heterogeneous nuclear ribonucleoprotein A2B1 (hnRNPA2B1) has been found to bind to m6A-bearing RNAs in vivo and in vitro .…”

Section: Introductionmentioning

confidence: 99%

“… 6 , 7 Hence, drug discovery that targets hnRNPA2/B1 could represent a novel strategy as overexpression of the hnRNPA2/B1 has been manifested in cancer. 8 Heterogeneous nuclear ribonucleoprotein A2B1 (hnRNPA2B1) has been found to bind to m6A-bearing RNAs in vivo and in vitro. 9 However, there is a lack of information on the nonsynonymous single nucleotide polymorphisms (nsSNPs) in hnRNPA2B1 and their association with RNA binding sites.…”

Section: Introductionmentioning

confidence: 99%

Analyzing the Effects of Single Nucleotide Polymorphisms on hnRNPA2/B1 Protein Stability and Function: Insights for Anticancer Therapeutic Design

Dutta,

Kravtsov,

Oleynikova

et al. 2024

ACS Omega

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Heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNPA2/B1) is a pivotal player in m6A recognition, RNA metabolism, and antiviral responses. In the context of cancer, overexpression of hnRNPA2/B1, abnormal RNA levels, and m6A depositions are evident. This study focuses on two significant nonsynonymous single nucleotide polymorphisms (nsSNPs) within hnRNPA2/B1, namely, F66L and E92K. Our structural analyses reveal decreased stability in these mutants, with E92K being predicted to undergo destabilizing post-translational methylation. Furthermore, our extensive analysis of 44,239 tumor samples from the COSMIC database uncovers that amino acid position 92 exhibits the second-highest mutation frequency within hnRNPA2/B1, particularly associated with breast and lung cancers. This experimental data aligns with our theoretical studies, highlighting the substantial impact of the nsSNP at position 92 on hnRNPA2/B1's stability and functionality. Given the critical role of pre-mRNA splicing, transcription, and translation regulation in cellular function, it is important to assess the impact of these nsSNPs on the stability and function of the hnRNPA2/B1 protein to design more efficient anticancer therapeutics.

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Emerging roles of hnRNP A2B1 in cancer and inflammation

Cited by 10 publications

References 191 publications

Pan‐cancer analysis of the oncogenic role of HNRNPR in human tumors

Pan‐cancer analysis of the oncogenic role of HNRNPR in human tumors

Roles of rRNA N‐methyladenosine modification in the function of ribosomes

Analyzing the Effects of Single Nucleotide Polymorphisms on hnRNPA2/B1 Protein Stability and Function: Insights for Anticancer Therapeutic Design

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