ArticleProceedings of the National Academy of Sciences of the United States of America1998
WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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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
60 citing papers in PubMed, 156 citations in OpenAlex.
- Selective and Potent First-in-Class CRBN-Dependent Molecular Glue Degraders of WW Domain-Binding Protein 4.Angewandte Chemie (International ed. in English) · 2026Article
- Exploration of phosphoproteomic association during epimorphic regeneration.Scientific reports · 2025Article
- Bi-allelic loss-of-function variants in WBP4, encoding a spliceosome protein, result in a variable neurodevelopmental syndrome.American journal of human genetics · 2023Article
- Pre-mRNA splicing factor U2AF2 recognizes distinct conformations of nucleotide variants at the center of the pre-mRNA splice site signal.Nucleic acids research · 2022Article
- Heterozygous loss of WBP11 function causes multiple congenital defects in humans and mice.Human molecular genetics · 2020Article
- The splicing-factor Prp40 affects dynein-dynactin function inMolecular biology of the cell · 2020Article
- E3 Ubiquitin ligase NEDD4 family‑regulatory network in cardiovascular disease.International journal of biological sciences · 2020Review
- Functional Consequences of theInternational journal of molecular sciences · 2019Article
- Delineating WWOX Protein Interactome by Tandem Affinity Purification-Mass Spectrometry: Identification of Top Interactors and Key Metabolic Pathways Involved.Frontiers in oncology · 2018Article
- A new role for FBP21 as regulator of Brr2 helicase activity.Nucleic acids research · 2017Article
- Prp40 Homolog A Is a Novel Centrin Target.Biophysical journal · 2017Article
- SAXS-Oriented Ensemble Refinement of Flexible Biomolecules.Biophysical journal · 2017Article
- Pharmacology of Modulators of Alternative Splicing.Pharmacological reviews · 2017Review
- Regulation of Skeletal Muscle Plasticity by Protein Arginine Methyltransferases and Their Potential Roles in Neuromuscular Disorders.Frontiers in physiology · 2017Review
- Article
- Ubiquitin ligase Nedd4-2 modulates Kv1.3 current amplitude and ion channel protein targeting.Journal of neurophysiology · 2016Article
- Determining structural ensembles of flexible multi-domain proteins using small-angle X-ray scattering and molecular dynamics simulations.Protein & cell · 2015Article
- Exploring monovalent and multivalent peptides for the inhibition of FBP21-tWW.Beilstein journal of organic chemistry · 2015Article
- Structure-guided U2AF65 variant improves recognition and splicing of a defective pre-mRNA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Hallmarks of alternative splicing in cancer.Oncogene · 2014Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pre-mRNA splicing requires the bridging of the 5' and 3' ends of the intron. In yeast, this bridging involves interactions between the WW domains in the splicing factor PRP40 and a proline-rich domain in the branchpoint binding protein, BBP. Using a proline-rich domain derived from formin (a product of the murine limb deformity locus), we have identified a family of murine formin binding proteins (FBP's), each of which contains one or more of a special class of tyrosine-rich WW domains. Two of these WW domains, in the proteins FBP11 and FBP21, are strikingly similar to those found in the yeast splicing factor PRP40. We show that FBP21 is present in highly purified spliceosomal complex A, is associated with U2 snRNPs, and colocalizes with splicing factors in nuclear speckle domains. Moreover, FBP21 interacts directly with the U1 snRNP protein U1C, the core snRNP proteins SmB and SmB', and the branchpoint binding protein SF1/mBBP. Thus, FBP21 may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex.
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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.