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非蛋白酶体泛素化调控MCF-7乳腺癌细胞中NCoR/SMRT/HDAC3共抑制复合物对染色质的占据。

Nonproteolytic ubiquitination regulates chromatin occupancy by the NCoR/SMRT/HDAC3 corepressor complex in MCF-7 breast cancer cells.

作者信息

Ferrero Giulio, Cardamone Maria Dafne, Luca Francesca, Bourk Eliot, Ricci Laura, Liu Wen, Gao Yuan, Burrone Giulia, Muhammad Akhirah, Chan Stefanie, Smith Emma, Fan Ting-Yu Claire, Cutrupi Santina, Garcia-Bassets Ivan, De Bortoli Michele, Rosenfeld Michael G, Perissi Valentina

机构信息

Department of Clinical and Biological Science, University of Torino, Orbassano (Torino) 10043, Italy.

Department of Biochemistry and Cell Biology, Chobanian and Avedisian School of Medicine, Boston University, Boston, MA 02118.

出版信息

Proc Natl Acad Sci U S A. 2025 May 6;122(18):e2502805122. doi: 10.1073/pnas.2502805122. Epub 2025 Apr 30.

Abstract

Tight regulation of gene expression is achieved through the coordinated action of transcription factors and cofactors that often can act as both repressors and activators in response to regulatory signals, with their activity modulated by context-specific signal transduction pathways that also impinge on their transient and cyclical recruitment to chromatin. However, the mechanisms underlying the intricate interplay between the regulatory strategies controlling cofactors' activity and localization across subcellar domains remain poorly understood. Here, we investigated the role of G-Protein Pathway Suppressor 2 (GPS2), a transcriptional cofactor critical for maintaining cellular homeostasis via regulation of mitochondrial biogenesis, stress response, lipid metabolism, insulin signaling, and inflammation, in MCF-7 breast cancer cells. By integration of biochemical assays with genome-wide RNA sequencing and Chromatin immunoprecipitation-Seq analyses, we show that nuclear GPS2 is required for licensing histone deacetylase 3 recruitment to chromatin via restricted ubiquitination by tumor necrosis factor receptor-associated factor 6 (TRAF6), an E3 ubiquitin ligase previously shown to regulate the switch from repressive to activating functions of the nuclear receptor corepressor (NCoR)/silencing mediator of retinoic acid and thyroid hormone receptor (SMRT) complex and here unexpectedly found to translocate to the nucleus in response to IL-1β stimulation. Nuclear TRAF6 is recruited to chromatin via direct interaction with the corepressors NCoR/SMRT, and TRAF6-mediated ubiquitination of TGF-beta activated kinase 1 (MAP3K7) binding protein 2 (TAB2), a facultative component of the NCoR/SMRT complex, contributes to corepressor clearance from target regulatory regions. Together, these results reveal an exquisite mechanism for coordinating the local regulation of cofactor activity with proinflammatory signaling pathways.

摘要

基因表达的严格调控是通过转录因子和辅因子的协同作用实现的,这些因子通常可作为阻遏物和激活物,响应调控信号,其活性由特定环境的信号转导途径调节,这些途径也影响它们向染色质的瞬时和周期性募集。然而,控制辅因子活性和跨亚细胞结构域定位的调控策略之间复杂相互作用的潜在机制仍知之甚少。在这里,我们研究了G蛋白信号通路抑制因子2(GPS2)在MCF-7乳腺癌细胞中的作用,GPS2是一种转录辅因子,通过调节线粒体生物发生、应激反应、脂质代谢、胰岛素信号传导和炎症来维持细胞内稳态。通过将生化分析与全基因组RNA测序和染色质免疫沉淀测序分析相结合,我们表明核GPS2是通过肿瘤坏死因子受体相关因子6(TRAF6)的限制性泛素化使组蛋白去乙酰化酶3募集到染色质所必需的,TRAF6是一种E3泛素连接酶,先前已证明其可调节核受体共抑制因子(NCoR)/视黄酸和甲状腺激素受体沉默介质(SMRT)复合物从抑制功能向激活功能的转变,并且在这里意外地发现其响应IL-1β刺激而转位至细胞核。核TRAF6通过与共抑制因子NCoR/SMRT直接相互作用被募集到染色质上,并且TRAF6介导的TGF-β激活激酶1(MAP3K7)结合蛋白2(TAB2)的泛素化,TAB2是NCoR/SMRT复合物的一个兼性成分,有助于共抑制因子从靶调控区域清除。总之,这些结果揭示了一种协调辅因子活性的局部调节与促炎信号通路的精妙机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e18/12067245/9aac60d65f76/pnas.2502805122fig01.jpg

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