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Crystal structure of CtBP1 in complex with PALI1
Structural highlights
FunctionCTBP1_HUMAN Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity.[1] [2] [3] [4] Publication Abstract from PubMedPolycomb Repressive Complex 2 (PRC2) and C-terminal binding proteins 1 and 2 (CtBP1/2) are key epigenetic regulators that frequently co-occupy chromatin, yet their crosstalk remains poorly understood. Here, we delineate the molecular basis of the interaction between CtBP1/2 and the N-terminal domain of PALI1, an accessory subunit of PRC2. The PALI1 N-terminus contains two DLS-like motifs that bind CtBP1/2 bivalently, enhancing affinity and promoting higher-order oligomerization. Conversely, disruption of CtBP1/2 oligomerization weakens PALI1 binding, revealing a reciprocal mechanism stabilizing the CtBP1/2-PALI1 complex. The 2.20 A structure of the CtBP1-PALI1 complex reveals the detailed interaction interface, which, together with biochemical data, supports a model where tandem DLS-like motifs drive CtBP1/2 oligomerization and multivalent engagement. Through its C-terminal PRC2-binding domain, PALI1 acts as a dual-interface scaffold linking CtBP1/2 and PRC2, providing a structural framework for their coordinated chromatin recruitment and transcriptional repression. PALI1 enhances CtBP1/2 oligomerization and couples CtBP1/2 to PRC2.,Zhang B, Jiang J, Chen P, Lin C, Sun W, Wang J, Li W, Chen J, Luo Q, Cai D, Cai Q, Chen S Biochem Biophys Res Commun. 2026 Feb 12;800:153295. doi: , 10.1016/j.bbrc.2026.153295. Epub 2026 Jan 14. PMID:41547303[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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