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The impact of the RBM4-initiated splicing cascade on modulating the carcinogenic signature of colorectal cancer cells.
hese findings suggest that RBM4 is a new biomarker in gastric cancer, as the reduced expression of this protein is correlated with poor differentiation, lymph node status and distant metastasis
RBM4-SRSF3-MAP4K4 constitutes a novel mechanism for manipulating the metastasis of colorectal cancer cells through the JNK1 signaling pathway.
TPM1-AS regulates the alternative splicing of TPM1 through an interaction with RBM4 and involves in TPM1-mediated filopodium formation and migration of cancer cells
RBM4 is induced and is involved in the PKM splicing switch and neuronal gene expression during hypoxia-induced neuronal differentiation.
alternative splicing patterns were altered by knockdown of RBM4 in several types of neoplasms
Loss of RBM4 expression is associated with colorectal cancer.
The results indicate that the alanine-rich C-terminal domain, in conjunction with its conjoined RNA-binding domain(s), differentially influences the subnuclear localization and biogenesis of RBM4.
Up-regulation of RBM4 is associated with breast cancer.
RBM4 is a tumor suppressor with therapeutic potential and clinical values as a prognostic factor.
we propose the emerging role of RBM4 in regulating the adipocyte-specific splicing events and transcription cascade, which subsequently facilitate the development and function of brown adipocyte-like cells.
role in negative feed-forward loop that disrupts inflammattory cytokine translation following Toll-like receptor 4 response
RBM4 homologs exert different effects on 5' splice site utilization and exon selection, and exhibit different subnuclear localization patterns.
RBM4 may synergize its effect on muscle cell-specific alternative splicing by down-regulating PTB expression and antagonizing the activity of PTB in exon selection
Data show that RBM4 interacts directly with Ago2 during muscle cell differentiation and may recruit Ago2 to suppress translation of target mRNAs.
Data show that the nuclear matrix protein matrin 3, cytoskeletal motor protein HMP, and the circadian clock protein lark were significantly decreased in fetal Down syndrome brain.
the regulated alternative splicing of alpha-TM by the antagonistic splicing regulators RBM4 and PTB
RBM4 is expressed in the human brain regions affected in tauopathy, including the hippocampus and frontal cortex. RBM4 is involved in tau exon 10 alternative splicing
Wilms tumor 1 protein, WT1 interacts with the novel splicing regulator RBM4, the longer isoform of WT1 is able to inhibit the effect of RBM4 on alternative splicing.
a previously unrecognized paradigm for the RNA-binding protein RBM4 in its phosphorylation-modulated dual action as a suppressor of cap-dependent and enhancer of IRES-mediated translation in response to stress signals
Study identified a novel splicing network composed of RBM4a, SRSF3, and MAP4K4 in brown adipogenesis and subsequently manipulating the effect of downstream JNK signaling which contributes to insulin resistance and reduced metabolism.
RBM4 depletion reduced the expression of the proneural gene Mash1, and such reduction was reversed by an RBM4-induced Numb isoform containing exon 3 but lacking exon 9. RBM4 was also essential for neurite outgrowth from cortical neurons in vitro. Neurite outgrowth defects of RBM4-depleted neurons were rescued by RBM4-induced exon 9-lacking Numb isoforms. RBM4 modulates exon selection of Numb.
RBM4a ablation enhanced the relative level of exon 4-excluded neuro-oncological ventral antigen 1 (Nova1(-4)) transcripts, which were predominantly generated in embryonic BAs
These results constitute a mechanistic understanding of the RBM4a-modulated splicing cascade during the brown adipogenesis.
The RBM4-MEF2C-miR-1 network constitutes a novel mechanism which programs the gene expression profile toward the development of brown adipocytes.
RBM4 overexpression was sufficient to convert AR42J cells into insulin-producing cells and may mediate glucose-induced insulin expression and insulin receptor isoform switches.
LARK ia a novel posttranscriptional regulator of the mammalian circadian clock.
RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of EIF2C2- containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG-3' motif in vitro (By similarity).
RNA binding motif protein 4
, RNA-binding motif protein 4.1
, RNA-binding protein 4.1
, RNA-binding motif protein 4a
, RNA-binding protein 4
, lark homolog
, transcriptional coactivator CoAZ
, zinc finger CCHC-type and RNA binding motif 3A
, RNA-binding motif protein 4