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Epigenetics from Oocytes to Embryos
Published in Carlos Simón, Carmen Rubio, Handbook of Genetic Diagnostic Technologies in Reproductive Medicine, 2022
Dagnė Daškevičiūtė, Marta Sanchez-Delgado, David Monk
As discussed above, for an embryo to develop beyond the initial reprogramming phase, the newly formed genome must be expressed. However, concurrent with ZGA/EGA is another equally important process, the degradation of maternal products (Figure 9.1b). These two events are not independent; rather, there is a complex interplay of maternal and zygotic factors in regulating various mechanistic aspects of MZT. In a similar fashion to transcriptional activation, the clearance of the maternally derived transcripts is a coordinated and gradual process during the initial stages of development (reviewed in 67). Some transcripts are eliminated soon after fertilization, whereas others are degraded only after the major onset of transcription during cleavage development. Maternal mRNA processing is controlled by a variety of different RNA-binding protein complexes, which recognize sequences in the maternal RNAs to promote their degradation via cleavage, deadenylation, and decapping. Recently, novel regulatory mechanisms, such as N6-methyladenosine RNA modifications,68 have been implicated as important determinants of RNA stability during the MZT.
Degenerative Diseases of the Nervous System
Published in Philip B. Gorelick, Fernando D. Testai, Graeme J. Hankey, Joanna M. Wardlaw, Hankey's Clinical Neurology, 2020
James A. Mastrianni, Elizabeth A. Harris
Pathologically, it is associated with diffuse brain atrophy with loss of cerebellar Purkinje's cells. Microscopically, degenerating areas of the brain demonstrate large ubiquitin positive intranuclear inclusions in glia and neurons.48 The FMR1 mRNA containing the expanded CGG repeat is thought to elicit neurodegeneration directly via a gain-of-function mechanism. The hypothesis is that the expanded CGG repeat binds to, and sequesters, certain RNA-binding proteins involved in RNA splicing, leading to aberrant splicing of other mRNAs.49
Introduction to Genomics
Published in Altuna Akalin, Computational Genomics with R, 2020
Some of the things that can be measured by high-throughput assays are as follows: Which genes are expressed and how much?Where does a transcription factor bind?Which bases are methylated in the genome?Which transcripts are translated?Where does RNA-binding proteins bind?Which microRNAs are expressed?Which parts of the genome are in contact with each other?Where are the mutations in the genome located?Which parts of the genome are nucleosome-free?
Transcription factor ETV1-induced lncRNA MAFG-AS1 promotes migration, invasion, and epithelial–mesenchymal transition of pancreatic cancer cells by recruiting IGF2BP2 to stabilize ETV1 expression
Published in Growth Factors, 2023
Hanqin Weng, Weijian Feng, Fengling Li, Dong Huang, Liangyi Lin, Zaiguo Wang
Based on the encouraging effect of MAFG-AS1 on EMT in PC, we further considered its downstream regulation mechanism. LncRNAs can sustain mRNA stability through RNA-binding protein (Bao et al. 2020; Wang et al. 2019). RNA-binding protein IGF2BP2 performs a regulatory role in EMT of PC (Dahlem et al. 2019). Thus, we speculated that MAFG-AS1 may participate in pancreatic EMT process by means of enrolling IGF2BP2 to maintain mRNA stability. As a result, we observed the enrichment of IGF2BP2 protein in MAFG-AS1 group. MAFG-AS1 was raised in the precipitation of anti-IGF2BP2, further confirming the binding relationship between MAFG-AS1 and IGF2BP2. However, there was no notable change in IGF2BP2 expression after MAFG-AS1 knockdown. It is noteworthy that IGF2BP2 serves as a reader for m6A-modified lncRNA DANCR and stabilizes DANCR RNA in PC (Hu et al. 2020). Our study first highlighted the interaction between MAFG-AS1 and IGF2BP2 in PC cells.
Emerging Drugs for the Treatment of Amyotrophic Lateral Sclerosis: A Focus on Recent Phase 2 Trials
Published in Expert Opinion on Emerging Drugs, 2020
Andrea Barp, Francesca Gerardi, Andrea Lizio, Valeria Ada Sansone, Christian Lunetta
There was a shift in focus to RNA dysregulation as a key of pathological process in ALS with the identification of disease-causing variations in RNA-binding protein genes, TARDBP [38], FUS [39,40], hnRNPA1 [41], MATR3 [42], TAF15 [43], and TIA1 [44]. Moreover, a variety of RNA binding factors are found sequestered in association with the hexanucleotide repeat expansion in the C9orf72 gene transcript [45–47]. Indeed, a misregulated splicing has been described in the cerebellum and frontal cortex of ALS patients with C9orf72 repeat expansion, as well as in sporadic patients [48]. RNA-binding proteins are involved in several aspects of RNA metabolism, including splicing, transcription, transport, translation, and storage in stress granules. These discoveries have led to an increased interest in the role of RNA metabolism in neurodegenerative diseases.
Regulating glycolysis, the TLR4 signal pathway and expression of RBM3 in mouse liver in response to acute cold exposure
Published in Stress, 2019
Hongzhao Shi, Ruizhi Yao, Shuai Lian, Peng Liu, Yang Liu, Yu Ying Yang, Huanmin Yang, Shize Li
Previous research has shown that the expression of RNA binding proteins is increased to resist an adverse environment by coordinating necessary intracellular translation and post-translational modification reactions. RNA binding protein 3 (RBM3), a member of the cold-inducible RNA binding protein family (Danno et al., 1997; Derry, Kerns, & Francke, 1995; Dresios et al., 2005; Jackson et al., 2015), has been clearly shown to be induced during hypoxia, cold stress, and ER stress (Jackson et al., 2015; Kita et al., 2002; Ryan, Morey, Ramsdell, & Van Dolah, 2005; Wellmann et al., 2004, 2010; Zhu, Zelmer, Kapfhammer, & Wellmann, 2016). The biological functions of RBM3 include the promotion of global protein synthesis, maintenance of the stability of mRNAs bearing AU-rich elements, induction of stemness via the glycogen synthase kinase (GSK)-3β/Wnt/β-catenin signaling pathway, promotion of skeletal muscle mass, modulation of the cell cycle in G2/M transition, and adjusting the biogenesis of many microRNAs during the Dicer step (Cok, Acton, Sexton, & Morrison, 2004; Ferry, Vanderklish, & Dupont-Versteegden, 2011; Matsuda et al., 2011; Pilotte, Dupont-Versteegden, & Vanderklish, 2011; Smart et al., 2007; Sureban et al., 2008; Venugopal et al., 2016; Wong et al., 2016). RBM3 has also been reported to participate in signaling pathways such as MAPK and serine/threonine kinase (also known as protein kinase B or PKB), all pointing to a general role of RBM3 in cell protection (Neutelings, Lambert, Nusgens, & Colige, 2013; Yang et al., 2017).