ArticleProceedings of the National Academy of Sciences of the United States of America2006
Combined top-down and bottom-up proteomics identifies a phosphorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 50 citations in OpenAlex.
- The RNA structural code: orchestrating gene expression and enabling precision therapies.Acta pharmacologica Sinica · 2026Review
- SLBP-independent control of maternal histone mRNA.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay.Nature communications · 2026Article
- Computational approaches to identify sites of phosphorylation.Proteomics · 2024Review
- Uridylation of the histone mRNA stem-loop weakens binding interactions with SLBP while maintaining interactions with 3'hExo.RNA biology · 2023Article
- A region of SLBP outside the mRNA-processing domain is essential for deposition of histone mRNA into theJournal of cell science · 2021Article
- ALYREF links 3'-end processing to nuclear export of non-polyadenylated mRNAs.The EMBO journal · 2019Article
- Birth and Death of Histone mRNAs.Trends in genetics : TIG · 2017Review
- Structure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome.Biochimica et biophysica acta · 2015Review
- Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.Biomolecules · 2015Review
- Structural basis for regulation of RNA-binding proteins by phosphorylation.ACS chemical biology · 2015Review
- Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.FEBS open bio · 2014Article
- Signaling pathways that control mRNA turnover.Cellular signalling · 2013Review
- Assembly of the SLIP1-SLBP complex on histone mRNA requires heterodimerization and sequential binding of SLBP followed by SLIP1.Biochemistry · 2013Article
- Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3'hExo ternary complex.Science (New York, N.Y.) · 2013Article
- The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination.Molecular and cellular biology · 2012Article
- Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars.Nature reviews. Drug discovery · 2012Review
- Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization.Biochemistry · 2012Article
- High-performance liquid chromatography separation and intact mass analysis of detergent-solubilized integral membrane proteins.Analytical biochemistry · 2011Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The stem-loop-binding protein (SLBP) is involved in multiple aspects of histone mRNA metabolism. To characterize the modification status and sites of SLBP, we combined mass spectrometric bottom-up (analysis of peptides) and top-down (analysis of intact proteins) proteomic approaches. Drosophilia SLBP is heavily phosphorylated, containing up to seven phosphoryl groups. Accurate M(r) determination by Fourier transform ion cyclotron resonance (FTICR)-MS and FTICR-MS top-down experiments using a variety of dissociation techniques show there is removal of the initiator methionine and acetylation of the N terminus in the baculovirus-expressed protein, and that T230 is stoichiometrically phosphorylated. T230 is highly conserved; we have determined that this site is also completely phosphorylated in baculovirus-expressed mammalian SLBP and extensively phosphorylated in both Drosophila and mammalian cultured cells. Removal of the phosphoryl group from T230 by either dephosphorylation or mutation results in a 7-fold reduction in the affinity of SLBP for the stem-loop RNA.
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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.