ArticleNucleic acids research2013
Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 36 citations in OpenAlex.
- Circularization and Ribosome Recycling: From Polysome Topology to Translational Control.International journal of molecular sciences · 2026Review
- Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay.Nature communications · 2026Article
- Ataxin-2-like promotes translation of nonpolyadenylated reovirus mRNA.Nature communications · 2025Article
- Eukaryotic initiation factor 4B is a multi-functional RNA binding protein that regulates histone mRNAs.Nucleic acids research · 2024Article
- HMGA1 Regulates the Expression of Replication-Dependent Histone Genes and Cell-Cycle in Breast Cancer Cells.International journal of molecular sciences · 2022Article
- Article
- Human cytomegalovirus lytic infection inhibits replication-dependent histone synthesis and requires stem loop binding protein function.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Functional Cyclization of Eukaryotic mRNAs.International journal of molecular sciences · 2020Article
- Stop codon context influences genome-wide stimulation of termination codon readthrough by aminoglycosides.eLife · 2020Article
- Revisiting the Closed-Loop Model and the Nature of mRNA 5'-3' Communication.Molecular cell · 2018Review
- Birth and Death of Histone mRNAs.Trends in genetics : TIG · 2017Review
- Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap binding.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Translation initiation mediated by nuclear cap-binding protein complex.BMB reports · 2017Review
- Influenza A Virus Polymerase Recruits the RNA Helicase DDX19 to Promote the Nuclear Export of Viral mRNAs.Scientific reports · 2016Article
- Stoichiometry and Change of the mRNA Closed-Loop Factors as Translating Ribosomes Transit from Initiation to Elongation.PloS one · 2016Article
- A multiprotein occupancy map of the mRNP on the 3' end of histone mRNAs.RNA (New York, N.Y.) · 2015Article
- A highly conserved region essential for NMD in the Upf2 N-terminal domain.Journal of molecular biology · 2014Article
- Structure and function of pre-mRNA 5'-end capping quality control and 3'-end processing.Biochemistry · 2014Article
- The C-terminal extension of Lsm4 interacts directly with the 3' end of the histone mRNP and is required for efficient histone mRNA degradation.RNA (New York, N.Y.) · 2014Article
- Replication stress-induced alternative mRNA splicing alters properties of the histone RNA-binding protein HBP/SLBP: a key factor in the control of histone gene expression.Bioscience reports · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
In metazoans, replication-dependent histone mRNAs end in a stem-loop structure instead of the poly(A) tail characteristic of all other mature mRNAs. This specialized 3' end is bound by stem-loop binding protein (SLBP), a protein that participates in the nuclear export and translation of histone mRNAs. The translational activity of SLBP is mediated by interaction with SLIP1, a middle domain of initiation factor 4G (MIF4G)-like protein that connects to translation initiation. We determined the 2.5 Å resolution crystal structure of zebrafish SLIP1 bound to the translation-activation domain of SLBP and identified the determinants of the recognition. We discovered a SLIP1-binding motif (SBM) in two additional proteins: the translation initiation factor eIF3g and the mRNA-export factor DBP5. We confirmed the binding of SLIP1 to DBP5 and eIF3g by pull-down assays and determined the 3.25 Å resolution structure of SLIP1 bound to the DBP5 SBM. The SBM-binding and homodimerization residues of SLIP1 are conserved in the MIF4G domain of CBP80/20-dependent translation initiation factor (CTIF). The results suggest how the SLIP1 homodimer or a SLIP1-CTIF heterodimer can function as platforms to bridge SLBP with SBM-containing proteins involved in different steps of mRNA metabolism.
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Registered trials
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.