ArticleThe Journal of biological chemistry2009
Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21).
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 47 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
- Systematic identification of germ granule proteins reveals specialized roles in RNAi and small RNA inheritance.Genes & development · 2026Article
- Systematic Identification of Germ Granule Proteins Reveals Specialized Roles in RNAi and Small RNA Inheritance.bioRxiv : the preprint server for biology · 2026Article
- Discovery and optimization of a synthetic small protein domain targeting antibodies.Frontiers in bioengineering and biotechnology · 2025Article
- Intramolecular autoinhibition regulates the selectivity of PRPF40A tandem WW domains for proline-rich motifs.Nature communications · 2024Article
- Probing the ligand binding specificity of FNBP4 WW domains and interaction with FH1 domain of FMN1.Current research in structural biology · 2024Article
- Bi-allelic loss-of-function variants in WBP4, encoding a spliceosome protein, result in a variable neurodevelopmental syndrome.American journal of human genetics · 2023Article
- The WW domain of IQGAP1 binds directly to the p110α catalytic subunit of PI 3-kinase.The Biochemical journal · 2023Article
- Modulating binding affinity, specificity, and configurations by multivalent interactions.Biophysical journal · 2022Article
- WW45 inhibits breast cancer cell proliferation by the Hedgehog signaling pathway.American journal of translational research · 2021Article
- Cytosolic sequestration of the vitamin D receptor as a therapeutic option for vitamin D-induced hypercalcemia.Nature communications · 2020Article
- Cooperative binding of the tandem WW domains of PLEKHA7 to PDZD11 promotes conformation-dependent interaction with tetraspanin 33.The Journal of biological chemistry · 2020Article
- The splicing-factor Prp40 affects dynein-dynactin function inMolecular biology of the cell · 2020Article
- Article
- A new role for FBP21 as regulator of Brr2 helicase activity.Nucleic acids research · 2017Article
- SAXS-Oriented Ensemble Refinement of Flexible Biomolecules.Biophysical journal · 2017Article
- Acute Simian Varicella Virus Infection Causes Robust and Sustained Changes in Gene Expression in the Sensory Ganglia.Journal of virology · 2016Article
- Determining structural ensembles of flexible multi-domain proteins using small-angle X-ray scattering and molecular dynamics simulations.Protein & cell · 2015Article
- Allostery mediates ligand binding to WWOX tumor suppressor via a conformational switch.Journal of molecular recognition : JMR · 2015Article
- Structural insights into the functional versatility of WW domain-containing oxidoreductase tumor suppressor.Experimental biology and medicine (Maywood, N.J.) · 2015Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human FBP21 (formin-binding protein 21) contains a matrin-type zinc finger and two tandem WW domains. It is a component of the spliceosomes and interacts with several established splicing factors. Here we demonstrate for the first time that FBP21 is an activator of pre-mRNA splicing in vivo and that its splicing activation function and interaction with the splicing factor SIPP1 (splicing factor that interacts with PQBP1 and PP1) are both mediated by the two tandem WW domains of group III. We determined the solution structure of the tandem WW domains of FBP21 and found that the WW domains recognize peptide ligands containing either group II (PPLP) or group III (PPR) motifs. The binding interfaces involve both the XP and XP2 grooves of the two WW domains. Significantly, the tandem WW domains of FBP21 are connected by a highly flexible region, enabling their simultaneous interaction with two proline-rich motifs of SIPP1. The strong interaction between SIPP1 and FBP21 can be explained by the conjugation of two low affinity interactions with the tandem WW domains. Our study provides a structural basis for understanding the molecular mechanism underlying the functional implication of FBP21 and the biological specificity of tandem WW domains.
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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.