Rbfox family proteins make the homo- and hetero-oligomeric complexes

Choi, Sunkyung; Kim, Yong-Eun; Kim, Jae Whan; Cho, Nam‐Joon; Cheon, Seonghye; Kim, Kee K.

doi:10.1016/j.bbrc.2017.11.128

Cited by 6 publications

(4 citation statements)

References 24 publications

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“…While some of the previous studies have highlighted the individual splicing activity of each member of the Rbfox family, the interactions among the Rbfox family members were unknown. Co-immunoprecipitation assays revealed that Rbfox proteins form both homo-and hetero-oligomeric complexes (Choi et al, 2018). Furthermore, an in vivo crosslinking approach confirmed that the Rbfox proteins form a dimer, which then assembles with other proteins to form a large multi-protein complex (Choi et al, 2018), thus, vindicating the results obtained from the 2016 study from Black's laboratory.…”

Section: Mechanism Of Splicing Regulation By Rbfoxmentioning

confidence: 55%

“…While some of the previous studies have highlighted the individual splicing activity of each member of the Rbfox family, the interactions among the Rbfox family members were unknown. Co‐immunoprecipitation assays revealed that Rbfox proteins form both homo‐ and hetero‐oligomeric complexes (Choi et al, 2018). Furthermore, an in vivo cross‐linking approach confirmed that the Rbfox proteins form a dimer, which then assembles with other proteins to form a large multi‐protein complex (Choi et al, 2018), thus, vindicating the results obtained from the 2016 study from Black's laboratory.…”

Section: Mechanism Of Splicing Regulation By Rbfoxmentioning

confidence: 99%

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To RNA‐binding and beyond: Emerging facets of the role of Rbfox proteins in development and disease

Mukherjee,

Nongthomba

2023

WIREs RNA

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The RNA‐binding Fox‐1 homologue (Rbfox) proteins represent an ancient family of splicing factors, conserved through evolution. All members share an RNA recognition motif (RRM), and a particular affinity for the GCAUG signature in target RNA molecules. The role of Rbfox, as a splice factor, deciding the tissue‐specific inclusion/exclusion of an exon, depending on its binding position on the flanking introns, is well known. Rbfox often acts in concert with other splicing factors, and forms splicing regulatory networks. Apart from this canonical role, recent studies show that Rbfox can also function as a transcription co‐factor, and affects mRNA stability and translation. The repertoire of Rbfox targets is vast, including genes involved in the development of tissue lineages, such as neurogenesis, myogenesis, and erythropoeiesis, and molecular processes, including cytoskeletal dynamics, and calcium handling. A second layer of complexity is added by the fact that Rbfox expression itself is regulated by multiple mechanisms, and, in vertebrates, exhibits tissue‐specific expression. The optimum dosage of Rbfox is critical, and its misexpression is etiological to various disease conditions. In this review, we discuss the contextual roles played by Rbfox as a tissue‐specific regulator for the expression of many important genes with diverse functions, through the lens of the emerging data which highlights its involvement in many human diseases. Furthermore, we explore the mechanistic details provided by studies in model organisms, with emphasis on the work with Drosophila.This article is categorized under: RNA Processing > Splicing Mechanisms RNA Interactions with Proteins and Other Molecules > Protein‐RNA Interactions: Functional Implications RNA Turnover and Surveillance > Regulation of RNA Stability RNA Processing > Splicing Regulation/Alternative Splicing

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Section: Mechanism Of Splicing Regulation By Rbfoxmentioning

confidence: 55%

“…While some of the previous studies have highlighted the individual splicing activity of each member of the Rbfox family, the interactions among the Rbfox family members were unknown. Co‐immunoprecipitation assays revealed that Rbfox proteins form both homo‐ and hetero‐oligomeric complexes (Choi et al, 2018). Furthermore, an in vivo cross‐linking approach confirmed that the Rbfox proteins form a dimer, which then assembles with other proteins to form a large multi‐protein complex (Choi et al, 2018), thus, vindicating the results obtained from the 2016 study from Black's laboratory.…”

Section: Mechanism Of Splicing Regulation By Rbfoxmentioning

confidence: 99%

To RNA‐binding and beyond: Emerging facets of the role of Rbfox proteins in development and disease

Mukherjee,

Nongthomba

2023

WIREs RNA

View full text Add to dashboard Cite

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“…The first enriched pathway detected in the NOCI group (Figure 2) involved RBFOX1 and RBFOX3, both of which play an important role in the nervous system. It is known that RBFOX family proteins interact, forming homo-and hetero-oligomeric complexes 11 . RBFOX1-3 knockout has been found to result in brain defects in cytoskeletal membranes and synaptic proteins 24 .…”

Section: Significantly Enriched Pathwaysmentioning

confidence: 99%

Genome-Wide Epigenomic Analyses in Patients With Nociceptive and Neuropathic Chronic Pain Subtypes Reveals Alterations in Methylation of Genes Involved in the Neuro-Musculoskeletal System

Stenz

Carré

Lüthi

et al. 2022

The Journal of Pain

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“…RBFOX1 is expressed in the central nervous system (CNS), heart and skeletal muscle, whereas RBFOX3 is exclusively expressed in postmitotic neurons of the CNS, and RBFOX2 is extensively expressed in various cell and tissue types (Chen et al ., 2016a; Damianov et al ., 2016; Gordon et al ., 2019). Studies on molecular and cellular functions of RBFOX3 have revealed that it is important for neural tissue development and physiologic function of the adult brain (Kim et al ., 2017; Choi et al ., 2018; Lin et al ., 2018). RBFOX2 is a master regulator of alternative splicing (Arya et al ., 2014).…”

Section: Introductionmentioning

confidence: 99%

RBFOX2 confers tumor growth by PI3K/AKT and MAPK signaling in gastric cancer

Xie

et al. 2023

European Journal of Cancer Prevention

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RNA-binding Fox (RBFOX)2, a member of a family of RNA-binding proteins, is well known as a regulator of alternative pre-mRNA splicing. However, its possible role in gastric cancer is unknown. In this study, we investigated the biologic role and clinical significance of RBFOX2 in gastric cancer growth and elucidated its underlying molecular mechanisms. We found that RBFOX2 was highly expressed in gastric cancer cell lines and tumor tissue compared with the adjacent nontumor tissue. We also found that RBFOX2 overexpression was correlated with poor overall survival in patients with gastric cancers. Multivariate survival analyses revealed that higher RBFOX2 expression was an independent prognostic factor for the overall survival of patients with gastric cancers. Suppression of RBFOX2 by shRNA inhibited gastric cancer cell proliferation, colony formation and induced apoptosis. Mechanism studies revealed that these effects were achieved through the simultaneous modulation of multiple signaling pathways. Knockdown of RBFOX2 expression by shRNA markedly inhibited the phosphorylation of phosphatidylinositol 3-hydroxy kinase, threonine kinase and extracellular signal-regulated kinase and Jun N-terminal kinases proteins. In contrast, the ectopic expression of RBFOX2 had the opposite effects. Moreover, RBFOX2 knockdown also induced the cleavage of caspase-3 and caspase-9 proteins. Collectively, these results demonstrate that RBFOX2 plays a critical role in regulating gastric cancer cell proliferation and survival and may be a potential prognostic biomarker and therapeutic target for gastric cancer.

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Rbfox family proteins make the homo- and hetero-oligomeric complexes

Cited by 6 publications

References 24 publications

To RNA‐binding and beyond: Emerging facets of the role of Rbfox proteins in development and disease

To RNA‐binding and beyond: Emerging facets of the role of Rbfox proteins in development and disease

Genome-Wide Epigenomic Analyses in Patients With Nociceptive and Neuropathic Chronic Pain Subtypes Reveals Alterations in Methylation of Genes Involved in the Neuro-Musculoskeletal System

RBFOX2 confers tumor growth by PI3K/AKT and MAPK signaling in gastric cancer

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