The Branchpoint Binding Protein

Rymond, Brian C.

doi:10.1007/978-1-4419-7005-3_9

Advances in Experimental Medicine and Biology

2010

DOI: 10.1007/978-1-4419-7005-3_9

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The Branchpoint Binding Protein

Brian C. Rymond

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Cited by 8 publications

(1 citation statement)

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“…The RES complex relies on intact splice site sequences, as well as the correct composition of RNA binding proteins to form an mRNP (16,17). Accordingly, mutations in genes encoding the Saccharomyces cerevisiae early splicing factors Mud2 and Msl5 result in a stalled commitment complex (16)(17)(18)(19)(20). Once the pre-mRNA is recognized as misprocessed, nuclear pore components such as the Mlp proteins are required for nuclear retention (21-23).…”

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Evolutionarily Conserved Polyadenosine RNA Binding Protein Nab2 Cooperates with Splicing Machinery To Regulate the Fate of Pre-mRNA

Soucek

Zeng

Bellur

et al. 2016

Molecular and Cellular Biology

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g Numerous RNA binding proteins are deposited onto an mRNA transcript to modulate posttranscriptional processing events ensuring proper mRNA maturation. Defining the interplay between RNA binding proteins that couple mRNA biogenesis events is crucial for understanding how gene expression is regulated. To explore how RNA binding proteins control mRNA processing, we investigated a role for the evolutionarily conserved polyadenosine RNA binding protein, Nab2, in mRNA maturation within the nucleus. This study reveals that nab2 mutant cells accumulate intron-containing pre-mRNA in vivo. We extend this analysis to identify genetic interactions between mutant alleles of nab2 and genes encoding a splicing factor, MUD2, and RNA exosome, RRP6, with in vivo consequences of altered pre-mRNA splicing and poly(A) tail length control. As further evidence linking Nab2 proteins to splicing, an unbiased proteomic analysis of vertebrate Nab2, ZC3H14, identifies physical interactions with numerous components of the spliceosome. We validated the interaction between ZC3H14 and U2AF2/U2AF 65 . Taking all the findings into consideration, we present a model where Nab2/ZC3H14 interacts with spliceosome components to allow proper coupling of splicing with subsequent mRNA processing steps contributing to a kinetic proofreading step that allows properly processed mRNA to exit the nucleus and escape Rrp6-dependent degradation. Gene expression is temporally and spatially regulated to produce a precise protein expression profile that dictates the function of each cell. Although much of this control occurs at the level of transcription, both co-and posttranscriptional events also play key regulatory roles. Newly synthesized mRNAs undergo numerous processing events, including 5= capping, splicing, 3=-end processing, and export to the cytoplasm (1, 2). Ensuring the synchrony of mRNA biogenesis requires RNA binding proteins that not only perform the processing tasks but also couple the events to ensure that only properly processed mRNAs are available for translation in the cytoplasm (3).Key processing events that must be coordinated include splicing and 3=-end processing. Although steps in mRNA processing are often depicted and studied as separate events, there is a growing body of evidence that these processing events are intimately coupled to one another (2). For example, splicing and 3=-end processing are coupled in humans as mutations in splice site and polyadenylation consensus sequences mutually disrupt both splicing and polyadenylation (4-6). In addition, a number of splicing factors copurify with the 3=-end processing complex (7-10). For example, there is evidence that the splicing factor U2AF2/ U2AF 65 functions as a bridge between the U2 snRNP and the 3=-end processing machinery (11,12). Given the extensive coupling between RNA processing steps, it is important to consider the consequences when one step of the process is disrupted in vivo. Cells have developed numerous overlapping mechanisms to ensure that faulty mRNA transcripts are not...

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confidence: 99%

Evolutionarily Conserved Polyadenosine RNA Binding Protein Nab2 Cooperates with Splicing Machinery To Regulate the Fate of Pre-mRNA

Soucek

Zeng

Bellur

et al. 2016

Molecular and Cellular Biology

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Intronic features that determine the selection of the 3′ splice site

Pérez-Valle

Vilardell

2012

WIREs RNA

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Most eukaryotic primary transcripts include segments, or introns, that will be accurately removed during RNA biogenesis. This process, known as pre‐messenger RNA splicing, is catalyzed by the spliceosome, accurately selecting a set of intronic marks from others apparently equivalent. This identification is critical, as incorrectly spliced RNAs can be toxic for the organism. One of these marks, the dinucleotide AG, signals the intronic 3′ end, or 3′ splice site (ss). In this review we will focus on those intronic features that have an impact on 3′ ss selection. These include the location and type of neighboring sequences, and their distance to the 3′ end. We will see that their interplay is needed to select the right intronic end, and that this can be modulated by additional intronic elements that contribute to alternative splicing, whereby diverse RNAs can be generated from identical precursors. This complexity, still poorly understood, is fundamental for the accuracy of gene expression. In addition, a clear knowledge of 3′ ss selection is needed to fully decipher the coding potential of genomes. WIREs RNA 2012 doi: 10.1002/wrna.1131 This article is categorized under: RNA Structure and Dynamics > Influence of RNA Structure in Biological Systems RNA Processing > Splicing Regulation/Alternative Splicing Regulatory RNAs/RNAi/Riboswitches > Riboswitches

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Splicing Factor Mutations in Myelodysplasias: Insights from Spliceosome Structures

Jenkins

Kielkopf

2017

Trends in Genetics

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Somatic mutations of pre-mRNA splicing factors recur among patients with myelodysplastic syndromes (MDS) and related malignancies. Although these MDS-relevant mutations alter splicing of a subset of transcripts, the mechanisms by which these single amino acid substitutions change gene expression remain controversial. New structures of spliceosome intermediates and associated protein complexes shed light on the molecular interactions mediated by “hotspots” of the SF3B1 and U2AF1 pre-mRNA splicing factors. The frequently mutated SF3B1 residues contact the pre-mRNA splice site. Based on structural-homology with other spliceosome subunits and recent findings of altered RNA binding by mutant U2AF1 proteins, we suggest that affected U2AF1 residues also contact pre-mRNA. Altered pre-mRNA recognition emerges as a molecular theme among MDS-relevant mutations of pre-mRNA splicing factors.

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The Branchpoint Binding Protein

Cited by 8 publications

References 152 publications

Evolutionarily Conserved Polyadenosine RNA Binding Protein Nab2 Cooperates with Splicing Machinery To Regulate the Fate of Pre-mRNA

Evolutionarily Conserved Polyadenosine RNA Binding Protein Nab2 Cooperates with Splicing Machinery To Regulate the Fate of Pre-mRNA

Intronic features that determine the selection of the 3′ splice site

Splicing Factor Mutations in Myelodysplasias: Insights from Spliceosome Structures

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