ArticleNucleic acids research2016
Structural basis for recruiting and shuttling of the spliceosomal deubiquitinase USP4 by SART3.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- Structures of Nicotiana benthamiana importin-α1 complexes reveal mechanisms for plant virus NLS recognition.The Plant journal : for cell and molecular biology · 2026Article
- Structural investigation of human U6 snRNA recognition by spliceosomal recycling factor SART3 RNA recognition motifs.The FEBS journal · 2026Article
- SART3 reads methylarginine-marked glycine- and arginine-rich motifs.Cell reports · 2024Article
- Crosstalk between ubiquitination and translation in neurodevelopmental disorders.Frontiers in molecular neuroscience · 2024Review
- Variants in SART3 cause a spliceosomopathy characterised by failure of testis development and neuronal defects.Nature communications · 2023Article
- Pro-apoptotic and anti-apoptotic regulation mediated by deubiquitinating enzymes.Cellular and molecular life sciences : CMLS · 2022Review
- Ubiquitination and Ubiquitin-Like Modifications as Mediators of Alternative Pre-mRNA Splicing inFrontiers in plant science · 2022Review
- Tip110/SART3-Mediated Regulation of NF-κB Activity by Targeting IκBα Stability Through USP15.Frontiers in oncology · 2022Article
- Serrate-Associated Protein 1, a splicing-related protein, promotes miRNA biogenesis in Arabidopsis.The New phytologist · 2021Article
- The Multifaceted Roles of USP15 in Signal Transduction.International journal of molecular sciences · 2021Review
- Spotlight on USP4: Structure, Function, and Regulation.Frontiers in cell and developmental biology · 2021Review
- USP15 Deubiquitinates TUT1 Associated with RNA Metabolism and Maintains Cerebellar Homeostasis.Molecular and cellular biology · 2020Article
- Analysis of copy number alterations reveals the lncRNA ALAL-1 as a regulator of lung cancer immune evasion.The Journal of cell biology · 2020Article
- Regulation of Deubiquitinating Enzymes by Post-Translational Modifications.International journal of molecular sciences · 2020Review
- Increased versatility despite reduced molecular complexity: evolution, structure and function of metazoan splicing factor PRPF39.Nucleic acids research · 2019Article
- TGF-β signaling pathway mediated by deubiquitinating enzymes.Cellular and molecular life sciences : CMLS · 2019Review
- The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel.The Journal of biological chemistry · 2018Article
- RNA-splicing factor SART3 regulates translesion DNA synthesis.Nucleic acids research · 2018Article
- The life of U6 small nuclear RNA, from cradle to grave.RNA (New York, N.Y.) · 2018Review
- CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing.Nature communications · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Squamous cell carcinoma antigen recognized by T-cells 3 (SART3) is a U4/U6 recycling factor as well as a targeting factor of USP4 and USP15. However, the details of how SART3 recognizes these deubiquitinases and how they get subsequently translocated into the nucleus are not known. Here, we present the crystal structures of the SART3 half-a-tetratricopeptide (HAT) repeat domain alone and in complex with the domain present in ubiquitin-specific protease (DUSP)-ubiquitin-like (UBL) domains of ubiquitin specific protease 4 (USP4). The 12 HAT repeats of SART3 are in two sub-domains (HAT-N and HAT-C) forming a dimer through HAT-C. USP4 binds SART3 at the opposite surface of the HAT-C dimer interface utilizing the β-structured linker between the DUSP and the UBL domains. The binding affinities of USP4 and USP15 to SART3 are 0.9 μM and 0.2 μM, respectively. The complex structure of SART3 nuclear localization signal (NLS) and importin-α reveals bipartite binding, and removal of SART3 NLS prevents the entry of USP4 (and USP15) into the nucleus and abrogates the subsequent deubiquitinase activity of USP4.
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