ArticleJournal of molecular biology2008
Structure of the N-terminal Mlp1-binding domain of the Saccharomyces cerevisiae mRNA-binding protein, Nab2.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- Intrinsically disordered regions facilitate Mlp1-Nab2 recognition in mRNA quality control.Nucleus (Austin, Tex.) · 2026Article
- The Polyadenosine RNA-Binding Protein ZC3H14 Localizes to Synapses and Regulates Synaptosomal CaMKIIα Levels.bioRxiv : the preprint server for biology · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- A kinetic ruler controls mRNA poly(A) tail length.Genes & development · 2025Article
- Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling.Nature communications · 2025Article
- Structure of the pre-mRNA leakage 39-kDa protein reveals a single domain of integrated zf-C3HC and Rsm1 modules.Scientific reports · 2022Article
- Mechanisms of nuclear mRNA export: A structural perspective.Traffic (Copenhagen, Denmark) · 2019Review
- Structure-function relationships in the Nab2 polyadenosine-RNA binding Zn finger protein family.Protein science : a publication of the Protein Society · 2019Review
- The multitasking polyA tail: nuclear RNA maturation, degradation and export.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- A Nuclear Export Block Triggers the Decay of Newly Synthesized Polyadenylated RNA.Cell reports · 2018Article
- The polyadenosine RNA-binding protein ZC3H14 interacts with the THO complex and coordinately regulates the processing of neuronal transcripts.Nucleic acids research · 2018Article
- The yeast Ty1 retrotransposon requires components of the nuclear pore complex for transcription and genomic integration.Nucleic acids research · 2018Article
- Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing.Nucleic acids research · 2017Article
- Structural basis for the dimerization of Nab2 generated by RNA binding provides insight into its contribution to both poly(A) tail length determination and transcript compaction in Saccharomyces cerevisiae.Nucleic acids research · 2017Article
- Links between mRNA splicing, mRNA quality control, and intellectual disability.RNA & disease (Houston, Tex.) · 2016Article
- The nuclear basket mediates perinuclear mRNA scanning in budding yeast.The Journal of cell biology · 2015Article
- Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2.Structure (London, England : 1993) · 2015Article
- Structural basis for the molecular recognition of polyadenosine RNA by Nab2 Zn fingers.Nucleic acids research · 2014Article
- Poly(A) tail-mediated gene regulation by opposing roles of Nab2 and Pab2 nuclear poly(A)-binding proteins in pre-mRNA decay.Molecular and cellular biology · 2013Article
- Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its function in mRNA nuclear export.Structure (London, England : 1993) · 2012Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Nuclear abundant poly(A) RNA-binding protein 2 (Nab2) is an essential yeast heterogeneous nuclear ribonucleoprotein that modulates both mRNA nuclear export and poly(A) tail length. The N-terminal domain of Nab2 (residues 1-97) mediates interactions with both the C-terminal globular domain of the nuclear pore-associated protein, myosin-like protein 1 (Mlp1), and the mRNA export factor, Gfd1. The solution and crystal structures of the Nab2 N-terminal domain show a primarily helical fold that is analogous to the PWI fold found in several other RNA-binding proteins. In contrast to other PWI-containing proteins, we find no evidence that the Nab2 N-terminal domain binds to nucleic acids. Instead, this domain appears to mediate protein:protein interactions that facilitate the nuclear export of mRNA. The Nab2 N-terminal domain has a distinctive hydrophobic patch centered on Phe73, consistent with this region of the surface being a protein:protein interaction site. Engineered mutations within this hydrophobic patch attenuate the interaction with the Mlp1 C-terminal domain but do not alter the interaction with Gfd1, indicating that this patch forms a crucial component of the interface between Nab2 and Mlp1.
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