SR Proteins and Related Factors in Alternative Splicing

Lin, Shengrong; Fu, Xiang‐Dong

doi:10.1007/978-0-387-77374-2_7

Cited by 187 publications

(187 citation statements)

References 160 publications

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“…The involvement of SRSF3 in the nutritional regulation of splicing is further supported by the regulation of SRSF3 phosphorylation and amount in response to insulin and arachidonic acid. Upon phosphorylation, SR proteins move from the cytoplasm to the nucleus and from sites of concentration within the nucleus, called speckles, to nascent RNA at transcription sites (8). In addition, phosphorylation enhances binding to RNA regulatory elements and protein-protein interactions (40,41).…”

Section: Discussionmentioning

confidence: 99%

“…The serines in the RS domains can be phosphorylated (6). Phosphorylation enhances the ability of the SR protein to recruit components of the spliceosome to splice sites, regulates the intracellular and intranuclear localization of SR proteins, and enhances the binding of the proteins to RNA (8). SR proteins are known to be substrates of several kinases including SRPK, Clk/Sty, and Akt and as such are candidates for mediating the impact of extracellular signals upon the splicing process (9 -11).…”

mentioning

confidence: 99%

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Serine Arginine Splicing Factor 3 Is Involved in Enhanced Splicing of Glucose-6-phosphate Dehydrogenase RNA in Response to Nutrients and Hormones in Liver

Walsh¹,

Suchanek²,

Cyphert

et al. 2013

Journal of Biological Chemistry

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Background: Regulation of G6PD expression by nutrients occurs by changes in accumulation of spliced mRNA without changes in transcriptional activity of the gene. Results: Refeeding enhances SRSF3 binding to G6PD mRNA. Loss of SRSF3 inhibits G6PD expression. Conclusion: SRSF3 is a target for nutritional regulation of splicing. Significance: Regulation of RNA splicing is a novel target for nutrient action.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Serine Arginine Splicing Factor 3 Is Involved in Enhanced Splicing of Glucose-6-phosphate Dehydrogenase RNA in Response to Nutrients and Hormones in Liver

Walsh¹,

Suchanek²,

Cyphert

et al. 2013

Journal of Biological Chemistry

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“…This is accomplished by a family of splicing commitment factors known as SR proteins, which are essential for multiple steps of spliceosome assembly in mammalian cells [55]. It is likely that, during transcriptional elongation, SR proteins and other spliceosomal components may be able to recognize emerging splicing signals in a timely manner in competition with other RNA binding proteins, such as hnRNP proteins, to nucleate the efficient assembly of functional spliceosomes on nascent transcripts [53].…”

Section: Functional Consequences Of Sequential Recognition Of Cis-actmentioning

confidence: 99%

Functional integration of transcriptional and RNA processing machineries

Pandit

Wang

2008

Current Opinion in Cell Biology

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153

134

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Co-transcriptional RNA processing not only permits temporal RNA processing before the completion of transcription, but also allows sequential recognition of RNA processing signals on nascent transcripts threading out from the elongating RNAPII complex. Rapid progress in recent years has established multiple contacts that physically connect the transcription and RNA processing machineries, which centers on the C-terminal domain (CTD) of the largest subunit of RNAPII. While co-transcriptional RNA processing has been substantiated, the evidence for "reciprocal" coupling starts to emerge, which emphasizes functional integration of transcription and RNA processing machineries in a mutually beneficial manner for efficient and regulated gene expression.

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“…Using the yeast two-hybrid system, the present study isolated a novel CypA-binding nuclear protein, SR-25. SR-25 is a novel member of a highly conserved family of splicing factors, the SR proteins (21,22). SR proteins are major modulators of alternative splicing, and usually contain a SR domain that is required for protein-protein interactions during splicing (23)(24)(25).…”

Section: Sr-25 Is Upregulated By Cypa Overexpression In Vitromentioning

confidence: 99%

Interaction of cyclophilin A with a novel binding protein, SR-25, and characterization of their expression pattern in Chinese hepatocellular carcinoma patients

Chen

Lian

et al. 2016

Oncology Letters

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Abstract. Cyclophilin (Cyp) A has been reported to be overexpressed in the majority of cancer cells, including hepatocellular carcinoma (HCC). However, the biological functions of CypA in HCC are far from being understood. To determine the biological functions of CypA in HCC, the present study screened human fetal liver complementary DNA for proteins interacting with CypA using the yeast two-hybrid system. A nuclear protein, serine/arginine-rich (SR)-25, was isolated as a novel CypA-binding protein that is distinct from those previously described in the literature. Binding assays and co-immunoprecipitation confirmed the physical association between CypA and SR-25. The present study demonstrated that CypA may interact with SR-25 through its peptidyl-prolyl isomerase domain. In addition, CypA may induce the expression of SR-25 in Hep3B cells. The messenger RNA levels of CypA and SR-25 in HCC indicated that there was a significant correlation between the expression of CypA and the expression of SR-25 in HCC. It can be speculated that the interaction between CypA and SR-25 proteins may be involved in potential carcinogenic functions of CypA in HCC. Further studies will focus on elucidating in detail the molecular mechanisms of the interaction between CypA and SR-25.

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SR Proteins and Related Factors in Alternative Splicing

Cited by 187 publications

References 160 publications

Serine Arginine Splicing Factor 3 Is Involved in Enhanced Splicing of Glucose-6-phosphate Dehydrogenase RNA in Response to Nutrients and Hormones in Liver

Serine Arginine Splicing Factor 3 Is Involved in Enhanced Splicing of Glucose-6-phosphate Dehydrogenase RNA in Response to Nutrients and Hormones in Liver

Functional integration of transcriptional and RNA processing machineries

Interaction of cyclophilin A with a novel binding protein, SR-25, and characterization of their expression pattern in Chinese hepatocellular carcinoma patients

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