ArticleProceedings of the National Academy of Sciences of the United States of America2019
Rotational symmetry of the structured Chip/LDB-SSDP core module of the Wnt enhanceosome.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Single-stranded DNA-binding proteins are essential components of the architectural LDB1 protein complex.Molecular cell · 2025Article
- Structural basis of the interaction between BCL9-Pygo and LDB-SSBP complexes in assembling the Wnt enhanceosome.Nature communications · 2023Article
- The WNT/β-catenin dependent transcription: A tissue-specific business.WIREs mechanisms of disease · 2021Review
- Mechanisms of Enhancer-Promoter Interactions in Higher Eukaryotes.International journal of molecular sciences · 2021Review
- The structural biology of canonical Wnt signalling.Biochemical Society transactions · 2020Review
- Crystal structure of human LDB1 in complex with SSBP2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The Chip/LIM-domain binding protein (LDB)-single-stranded DNA-binding protein (SSDP) (ChiLS) complex controls numerous cell-fate decisions in animal cells, by mediating transcription of developmental control genes via remote enhancers. ChiLS is recruited to these enhancers by lineage-specific LIM-domain proteins that bind to its Chip/LDB subunit. ChiLS recently emerged as the core module of the Wnt enhanceosome, a multiprotein complex that primes developmental control genes for timely Wnt responses. ChiLS binds to NPFxD motifs within Pygopus (Pygo) and the Osa/ARID1A subunit of the BAF chromatin remodeling complex, which could synergize with LIM proteins in tethering ChiLS to enhancers. Chip/LDB and SSDP both contain N-terminal dimerization domains that constitute the bulk of their structured cores. Here, we report the crystal structures of these dimerization domains, in part aided by DARPin chaperones. We conducted systematic surface scanning by structure-designed mutations, followed by in vitro and in vivo binding assays, to determine conserved surface residues required for binding between Chip/LDB, SSDP, and Pygo-NPFxD. Based on this, and on the 4:2 (SSDP-Chip/LDB) stoichiometry of ChiLS, we derive a highly constrained structural model for this complex, which adopts a rotationally symmetrical SSDP
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