Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression
By D. A. Mangus, Matthew C Evans, A. Jacobson. Genome Biology, 2003
646 citations recorded by the source corpus.
SummaryMost eukaryotic mRNAs are subject to considerable post-transcriptional modification, including capping, splicing, and polyadenylation. The process of polyadenylation adds a 3' poly(A) tail and provides the mRNA with a binding site for a major class of regulatory factors, the poly(A)-binding proteins (PABPs). These highly conserved polypeptides are found only in eukaryotes; single-celled eukaryotes each have a single PABP, whereas humans have five and Arabidopis has eight. They typically bind poly(A) using one or more RNA-recognition motifs, globular domains common to numerous other eukaryotic RNA-binding proteins. Although they lack catalytic activity, PABPs have several roles in mediating gene expression. Nuclear PABPs are necessary for the synthesis of the poly(A) tail, regulating its ultimate length and stimulating maturation of the mRNA. Association with PABP is also a requirement for some mRNAs to be exported from the nucleus. In the cytoplasm, PABPs facilitate the formation of the 'closed loop' structure of the messenger ribonucleoprotein particle that is crucial for additional PABP activities that promote translation initiation and termination, recycling of ribosomes, and stability of the mRNA. Collectively, these sequential nuclear and cytoplasmic contributions comprise a cycle in which PABPs and the poly(A) tail first create and then eliminate a network of cis- acting interactions that control mRNA function.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/7dec50ab0c39969cf8da9d03cbdc037af57fb5bd
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Citations in the corpus
- AU-rich elements and associated factors: are there unifying principles? (2006, background): “This relationship has also been observed in many lower and higher eukaryotes [reviewed in (141)].”
- Advance Publication by J-STAGE Japanese Journal of Infectious Diseases Isolation of human coronaviruses OC43, HKU1, NL63, and 229E in Yamagata, Japan, using primary human airway epithelium cells cultured by employing an air-liquid interface culture (2020, neutral): “Cytoplasmic PABPs, including Pabpc1, Epab, and Pabpc2 (known as PABPC3 in humans), are composed of three major domains: four RNA recognition motifs (RRMs) at the N-terminus, a proline-rich region, and a PABC domain at the C-terminus [30, 31].”
- Combining Natural Sequence Variation with High Throughput Mutational Data to Reveal Protein Interaction Sites (2015, background): “The eukaryotic poly(A)-binding protein regulates mRNA translation and decay [17,18,19] by binding to the poly(A) tail of an mRNA via its four RRMs [20,21].”
- Deep mutational scanning of an RRM domain of the Saccharomyces cerevisiae poly(A)-binding protein (2013, background): “This ∼90-amino acid domain is present in proteins with roles in post-transcriptional processes such as pre-mRNA processing, mRNA nuclear export, translational regulation, and mRNA decay (Mangus et al. 2003; Erkmann and Kutay 2004; DeschenesFurry et al. 2006; Kuhn et al. 2009).”