Structural basis for mRNA recognition by human RBM38

Qian, Kaiyue; Li, Mengyu; Wang, Junchao; Zhang, Min; Wang, Mingzhu

doi:10.1042/bcj20190652

Cited by 9 publications

(5 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, it is almost identical to the RRM of Rbm38, such that both Rbm24 and Rbm38 prefers similar GU-rich sequences in target mRNAs [ 21 , 24 ]. Although the sequence outside the RRM is relatively divergent, at least two conserved domains can be identified in the C-terminal half of vertebrate Rbm24 and Rbm38 [ 25 ].…”

Section: Rbm24 Functional Domainsmentioning

confidence: 99%

“…Alterations in protein–RNA interactions have been causally related to the occurrence of various cancers in humans [ 9 ]. Since Rbm24 protein contains a canonical RRM that binds to the GU-rich ligand present in a wide spectrum of target mRNAs [ 21 , 24 ], it would be not surprising that inappropriate regulation of its expression or function in humans perturbs the homeostasis of protein synthesis and leads to cancer development. There is accumulating evidence that Rbm24 displays tumor repressive activity.…”

Section: Potential Implication Of Rbm24 In Diseasementioning

confidence: 99%

See 1 more Smart Citation

RNA-Binding Protein Rbm24 as a Multifaceted Post-Transcriptional Regulator of Embryonic Lineage Differentiation and Cellular Homeostasis

Grifone

Shao

Saquet

et al. 2020

Cells

View full text Add to dashboard Cite

RNA-binding proteins control the metabolism of RNAs at all stages of their lifetime. They are critically required for the post-transcriptional regulation of gene expression in a wide variety of physiological and pathological processes. Rbm24 is a highly conserved RNA-binding protein that displays strongly regionalized expression patterns and exhibits dynamic changes in subcellular localization during early development. There is increasing evidence that it acts as a multifunctional regulator to switch cell fate determination and to maintain tissue homeostasis. Dysfunction of Rbm24 disrupts cell differentiation in nearly every tissue where it is expressed, such as skeletal and cardiac muscles, and different head sensory organs, but the molecular events that are affected may vary in a tissue-specific, or even a stage-specific manner. Recent works using different animal models have uncovered multiple post-transcriptional regulatory mechanisms by which Rbm24 functions in key developmental processes. In particular, it represents a major splicing factor in muscle cell development, and plays an essential role in cytoplasmic polyadenylation during lens fiber cell terminal differentiation. Here we review the advances in understanding the implication of Rbm24 during development and disease, by focusing on its regulatory roles in physiological and pathological conditions.

show abstract

Section: Rbm24 Functional Domainsmentioning

confidence: 99%

Section: Potential Implication Of Rbm24 In Diseasementioning

confidence: 99%

RNA-Binding Protein Rbm24 as a Multifaceted Post-Transcriptional Regulator of Embryonic Lineage Differentiation and Cellular Homeostasis

Grifone

Shao

Saquet

et al. 2020

Cells

View full text Add to dashboard Cite

show abstract

“…Both forms are expressed in the nucleus and cytoplasm, and the N-terminal sequences are identical. The RBM38 protein contains a highly conserved RRM (amino acids 35-107) 31 and four introns (amino acids 79, 120, 138 and 239). In the human RBM38 gene, 34 functional single nucleotide polymorphisms (SNPs) have been identified, 14 of which cause missense mutations, 12 of which cause nonsense mutations, and 8 of which cause exon splicing enhanced mutations.…”

Section: The Structure Of Rbm38mentioning

confidence: 99%

RNA-Binding Motif Protein 38 as a Potential Biomarker and Therapeutic Target in Cancer

She¹,

Lin²,

Liang³

et al. 2020

OTT

View full text Add to dashboard Cite

RNA-binding proteins (RBPs) act as a key factor in gene regulation by governing RNA metabolism. They contribute to the expression and functions of most RNAs by binding to them and forming complexes. RNA-binding motif protein 38 (RBM38), a member of the RBP family, alters the stability and translation of targeted mRNAs to affect various biological processes, such as cell proliferation, cell cycle arrest, and myogenic differentiation. RBM38 contains a highly conserved RNA recognition motif (RRM) consisting of two subunits, RNP1 and RNP2, which specifically bind to RNAs. Recent studies have revealed that RBM38 regulates the mRNA stability of several tumor-related genes, such as p53 , mdm2 , p63 , p73 , p21 , and c-Myc , by binding to their 3′ untranslated regions (3′ UTRs); thus, RBM38 modulates targeted gene expression and affects the biological processes of tumors. In addition, abnormal RBM38 expression in some malignant tumors and its correlation with prognosis have been documented in many studies, indicating its value for potential clinical applications. In this review, we present an overview of RBM38, specifically highlighting its relationship with tumor manifestation and development. A brief overview of the potential use of RBM38 in cancer therapy is also included to provide ideas for further research on RBM38.

show abstract

“…Therefore, RBPs are involved in the posttranscriptional upregulation and downregulation of multiple tumor-suppressor genes and oncogenes, which may lead to tumorigenesis and the progression of human cancers [15]. The RNA-binding motif protein 38 (RBM38) is a member of the RNA recognition motif family of RBPs; the gene which encodes RBM38 is located on chromosome 20q13, and is downregulated in various cancer tissues [16]. RBM38 contains a classical RNA recognition motif (RRM) domain, and binds to transcripts which contain AU-or U-rich elements, which facilitates post-transcriptional regulation of numerous downstream proteins [16].…”

Section: Introductionmentioning

confidence: 99%

“…The RNA-binding motif protein 38 (RBM38) is a member of the RNA recognition motif family of RBPs; the gene which encodes RBM38 is located on chromosome 20q13, and is downregulated in various cancer tissues [16]. RBM38 contains a classical RNA recognition motif (RRM) domain, and binds to transcripts which contain AU-or U-rich elements, which facilitates post-transcriptional regulation of numerous downstream proteins [16]. Therefore, it plays a key role in various biological functions, including cell proliferation, apoptosis, migration, and invasion [17,18].…”

Section: Introductionmentioning

confidence: 99%

RBM38 Reverses Sorafenib Resistance in Hepatocellular Carcinoma Cells by Combining and Promoting lncRNA-GAS5

Gao

Lü

Liu

et al. 2023

Cancers

View full text Add to dashboard Cite

Background: Hepatocellular carcinoma (HCC) is a life-threatening human malignancy and the fourth leading cause of cancer-related deaths worldwide. Patients with HCC are often diagnosed at an advanced stage with a poor prognosis. Sorafenib is a multikinase inhibitor used as the first-line treatment for patients with advanced HCC. However, acquired resistance to sorafenib in HCC leads to tumor aggression and limits the drug’s survival benefits; the underlying molecular mechanisms for this resistance remain unclear. Methods: This study aimed to examine the role of the tumor suppressor RBM38 in HCC, and its potential to reverse sorafenib resistance. In addition, the molecular mechanisms underlying the binding of RBM38 and the lncRNA GAS5 were examined. The potential involvement of RBM38 in sorafenib resistance was examined using both in vitro and in vivo models. Functional assays were performed to assess whether RBM38: binds to and promotes the stability of the lncRNA GAS5; reverses the resistance of HCC to sorafenib in vitro; and suppresses the tumorigenicity of sorafenib-resistant HCC cells in vivo. Results: RBM38 expression was lower in HCC cells. The IC50 value of sorafenib was significantly lower in cells with RBM38 overexpression than in control cells. RBM38 overexpression improved sorafenib sensitivity in ectopic transplanted tumors and suppressed the growth rate of tumor cells. RBM38 could bind to and stabilize GAS5 in sorafenib-resistant HCC cells. In addition, functional assays revealed that RBM38 reversed sorafenib resistance both in vivo and in vitro in a GAS5-dependent manner. Conclusions: RBM38 is a novel therapeutic target that can reverse sorafenib resistance in HCC by combining and promoting the lncRNA GAS5.

show abstract

Structural basis for mRNA recognition by human RBM38

Cited by 9 publications

References 39 publications

RNA-Binding Protein Rbm24 as a Multifaceted Post-Transcriptional Regulator of Embryonic Lineage Differentiation and Cellular Homeostasis

RNA-Binding Protein Rbm24 as a Multifaceted Post-Transcriptional Regulator of Embryonic Lineage Differentiation and Cellular Homeostasis

RNA-Binding Motif Protein 38 as a Potential Biomarker and Therapeutic Target in Cancer

RBM38 Reverses Sorafenib Resistance in Hepatocellular Carcinoma Cells by Combining and Promoting lncRNA-GAS5

Contact Info

Product

Resources

About