ArticleThe Journal of biological chemistry2014
Crystal structure of the ubiquitin-like domain-CUT repeat-like tandem of special AT-rich sequence binding protein 1 (SATB1) reveals a coordinating DNA-binding mechanism.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Expanding Clinical and Genetic Landscape ofGenes · 2025Article
- Article
- CUT homeobox genes: transcriptional regulation of neuronal specification and beyond.Frontiers in cellular neuroscience · 2023Review
- A novel SATB1 protein isoform with different biophysical properties.Frontiers in cell and developmental biology · 2023Article
- The 3D enhancer network of the developing T cell genome is shaped by SATB1.Nature communications · 2022Article
- ZFP451-mediated SUMOylation of SATB2 drives embryonic stem cell differentiation.Genes & development · 2021Article
- Global chromatin organizer SATB1 acts as a context-dependent regulator of the Wnt/Wg target genes.Scientific reports · 2021Article
- SATB2-LEMD2 interaction links nuclear shape plasticity to regulation of cognition-related genes.The EMBO journal · 2021Article
- SATB1-mediated chromatin landscape in T cells.Nucleus (Austin, Tex.) · 2020Review
- Tetramerization of SATB1 is essential for regulating of gene expression.Molecular and cellular biochemistry · 2017Article
- Satb2 determines miRNA expression and long-term memory in the adult central nervous system.eLife · 2016Article
- Homeodomain proteins: an update.Chromosoma · 2016Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SATB1 is essential for T-cell development and growth and metastasis of multitype tumors and acts as a global chromatin organizer and gene expression regulator. The DNA binding ability of SATB1 plays vital roles in its various biological functions. We report the crystal structure of the N-terminal module of SATB1. Interestingly, this module contains a ubiquitin-like domain (ULD) and a CUT repeat-like (CUTL) domain (ULD-CUTL tandem). Detailed biochemical experiments indicate that the N terminus of SATB1 (residues 1-248, SATB1((1-248))), including the extreme 70 N-terminal amino acids, and the ULD-CUTL tandem bind specifically to DNA targets. Our results show that the DNA binding ability of full-length SATB1 requires the contribution of the CUTL domain, as well as the CUT1-CUT2 tandem domain and the homeodomain. These findings may reveal a multiple-domain-coordinated mechanism whereby SATB1 recognizes DNA targets.
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