ArticleStructure (London, England : 1993)2012
Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its function in mRNA nuclear export.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- A kinetic ruler controls mRNA poly(A) tail length.Genes & development · 2025Article
- Defenders of the Transcriptome: Guard Protein-Mediated mRNA Quality Control inInternational journal of molecular sciences · 2024Review
- Genome-wide identification of Sclerotinia sclerotiorum small RNAs and their endogenous targets.BMC genomics · 2023Article
- Structure of the pre-mRNA leakage 39-kDa protein reveals a single domain of integrated zf-C3HC and Rsm1 modules.Scientific reports · 2022Article
- Three-layered control of mRNA poly(A) tail synthesis inGenes & development · 2021Article
- PIN and CCCH Zn-finger domains coordinate RNA targeting in ZC3H12 family endoribonucleases.Nucleic acids research · 2021Article
- AlphaScreen Identifies MSUT2 Inhibitors for Tauopathy-Targeting Therapeutic Discovery.SLAS discovery : advancing life sciences R & D · 2021Article
- Targeting Pathological Tau by Small Molecule Inhibition of the Poly(A):MSUT2 RNA-Protein Interaction.ACS chemical neuroscience · 2020Article
- Structure-function relationships in the Nab2 polyadenosine-RNA binding Zn finger protein family.Protein science : a publication of the Protein Society · 2019Review
- Polyadenylation and nuclear export of mRNAs.The Journal of biological chemistry · 2019Review
- The RNA-binding protein, ZC3H14, is required for proper poly(A) tail length control, expression of synaptic proteins, and brain function in mice.Human molecular genetics · 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
- The Evolutionarily-conserved Polyadenosine RNA Binding Protein, Nab2, Cooperates with Splicing Machinery to Regulate the Fate of pre-mRNA.Molecular and cellular biology · 2016Article
- An amyotrophic lateral sclerosis-linked mutation in GLE1 alters the cellular pool of human Gle1 functional isoforms.Advances in biological regulation · 2016Article
- Recognition of distinct RNA motifs by the clustered CCCH zinc fingers of neuronal protein Unkempt.Nature structural & molecular biology · 2016Article
- The poly(A)-binding protein Nab2 functions in RNA polymerase III transcription.Genes & development · 2015Article
- Nucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complex.Genetics · 2014Article
- Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation.The EMBO journal · 2014Article
- Article
- Structural basis for the molecular recognition of polyadenosine RNA by Nab2 Zn fingers.Nucleic acids research · 2014Article
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11 authors at 3 institutions in 2 countries.
Funding
Abstract
Polyadenylation regulation and efficient nuclear export of mature mRNPs both require the polyadenosine-RNA-binding protein, Nab2, which contains seven CCCH Zn fingers. We describe here the solution structure of fingers 5-7, which are necessary and sufficient for high-affinity polyadenosine-RNA binding, and identify key residues involved. These Zn fingers form a single structural unit. Structural coherence is lost in the RNA-binding compromised Nab2-C437S mutant, which also suppresses the rat8-2 allele of RNA helicase Dbp5. Structure-guided Nab2 variants indicate that dbp5(rat8-2) suppression is more closely linked to hyperadenylation and suppression of mutant alleles of the nuclear RNA export adaptor, Yra1, than to affinity for polyadenosine-RNA. These results indicate that, in addition to modulating polyA tail length, Nab2 has an unanticipated function associated with generating export-competent mRNPs, and that changes within fingers 5-7 lead to suboptimal assembly of mRNP export complexes that are more easily disassembled by Dbp5 upon reaching the cytoplasm.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.