ArticleThe Journal of biological chemistry2011
CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- Mechanism and regulation of secondary immunoglobulin diversification.Cell cycle (Georgetown, Tex.) · 2023Review
- The PRP19 Ubiquitin Ligase, Standing at the Cross-Roads of mRNA Processing and Genome Stability.Cancers · 2022Review
- Disease-associated CTNNBL1 mutation impairs somatic hypermutation by decreasing nuclear AID.The Journal of clinical investigation · 2020Article
- Article
- Light-induced injury in mouse embryos revealed by single-cell RNA sequencing.Biological research · 2019Article
- APOBEC3H Subcellular Localization Determinants Define Zipcode for Targeting HIV-1 for Restriction.Molecular and cellular biology · 2018Article
- Article
- Metazoan evolution of the armadillo repeat superfamily.Cellular and molecular life sciences : CMLS · 2017Article
- Charactering the ZFAND3 gene mapped in the sex-determining locus in hybrid tilapia (Oreochromis spp.).Scientific reports · 2016Article
- CTNNBL1 facilitates the association of CWC15 with CDC5L and is required to maintain the abundance of the Prp19 spliceosomal complex.Nucleic acids research · 2015Article
- Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin α.FEBS letters · 2014Article
- BIMMER: a novel algorithm for detecting differential DNA methylation regions from MBDCap-seq data.BMC bioinformatics · 2014Article
- Deficiency in spliceosome-associated factor CTNNBL1 does not affect ongoing cell cycling but delays exit from quiescence and results in embryonic lethality in mice.Cell cycle (Georgetown, Tex.) · 2013Article
- RNA profiles of porcine embryos during genome activation reveal complex metabolic switch sensitive to in vitro conditions.PloS one · 2013Article
- Cep164 mediates vesicular docking to the mother centriole during early steps of ciliogenesis.The Journal of cell biology · 2012Article
- A role for the RNA pol II-associated PAF complex in AID-induced immune diversification.The Journal of experimental medicine · 2012Article
- Three-dimensional architecture of the IgH locus facilitates class switch recombination.Annals of the New York Academy of Sciences · 2012Article
- AID targeting is dependent on RNA polymerase II pausing.Seminars in immunology · 2012Review
- APOBEC3B and AID have similar nuclear import mechanisms.Journal of molecular biology · 2012Article
- Functions and regulation of the APOBEC family of proteins.Seminars in cell & developmental biology · 2012Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Nuclear proteins typically contain short stretches of basic amino acids (nuclear localization sequences; NLSs) that bind karyopherin α family members, directing nuclear import. Here, we identify CTNNBL1 (catenin-β-like 1), an armadillo motif-containing nuclear protein that exhibits no detectable primary sequence homology to karyopherin α, as a novel, selective NLS-binding protein. CTNNBL1 (a single-copy gene conserved from fission yeast to man) was previously found associated with Prp19-containing RNA-splicing complexes as well as with the antibody-diversifying enzyme AID. We find that CTNNBL1 association with the Prp19 complex is mediated by recognition of the NLS of the CDC5L component of the complex and show that CTNNBL1 also interacts with Prp31 (another U4/U6.U5 tri-snRNP-associated splicing factor) through its NLS. As with karyopherin αs, CTNNBL1 binds NLSs via its armadillo (ARM) domain, but displays a separate, more selective NLS binding specificity. Furthermore, the CTNNBL1/AID interaction depends on amino acids forming the AID conformational NLS with CTNNBL1-deficient cells showing a partial defect in AID nuclear accumulation. However, in further contrast to karyopherin αs, the CTNNBL1 N-terminal region itself binds karyopherin αs (rather than karyopherin β), suggesting a function divergent from canonical nuclear transport. Thus, CTNNBL1 is a novel NLS-binding protein, distinct from karyopherin αs, with the results suggesting a possible role in the selective intranuclear targeting or interactions of some splicing-associated complexes.
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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.