Abstract
Signal transduction and the regulation of gene expression are fundamental processes in every cell. RNA-binding proteins (RBPs) play a key role in the post-transcriptional modulation of gene expression in response to both internal and external stimuli. However, how signaling pathways regulate the assembly of RBPs with mRNAs remains largely unknown. Here, we summarize observations showing that the formation and composition of messenger ribonucleoprotein particles (mRNPs) is dynamically remodeled in space and time by specific signaling cascades and the resulting post-translational modifications. The integration of signaling events with gene expression is key to the rapid adaptation of cells to environmental changes and stress. Only a combined approach analyzing the signal transduction pathways and the changes in post-transcriptional gene expression they cause will unravel the mechanisms coordinating these important cellular processes.
Highlights
Gene expression is a multi-step process involving the synthesis of the messenger (m)RNA during transcription followed by mRNA processing, export to the cytoplasm, protein synthesis and mRNA decay [1]
The mRNA exporter Mex67-Mtr2/NXF1-NXT1 directly binds to components of the nuclear pore complex (NPC) and transports the messenger ribonucleoprotein particles (mRNPs) through the NPC to the cytoplasm [84]
Many studies showed a functional relevance of arginine methylation for phase separation and RNP function, but these studies are experimentally challenging given that (I) the methylation-mimicking or -deficient status cannot be faithfully reproduced by amino acid mutations, (II) interference with writers or erasers of arginine methylation necessarily affects a large number of different substrates and does not allow conclusions on the function of one particular residue, and (III) antibodies detecting individual arginine methylation sites are rarely available
Summary
Gene expression is a multi-step process involving the synthesis of the messenger (m)RNA during transcription followed by mRNA processing, export to the cytoplasm, protein synthesis and mRNA decay [1]. TREX is recruited to the 5 as well as the 3 end of the mRNA by the interaction of ALYREF with the CBC and PABPN1 (polyA-binding protein nuclear 1), respectively [12,61,62] This is consistent with the interaction of the ALYREF homolog Yra with Pcf, a component of the cleavage and polyadenylation complex [63]. Several SR proteins are components of nuclear mRNPs. In yeast, the SR-like protein Npl is already recruited to the transcription machinery, associates with the mRNA co-transcriptionally and functions in transcription elongation, splicing, 3 end formation and nuclear mRNA export [55,70,71,72,73]. Nuclear mRNP assembly is tightly integrated within the gene expression pathway
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