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PARP7 和单 ADP-核糖基化负调控人乳腺癌细胞中的雌激素受体 α 信号转导。

PARP7 and Mono-ADP-Ribosylation Negatively Regulate Estrogen Receptor α Signaling in Human Breast Cancer Cells.

机构信息

Department of Nutrition, Institute of Basic Medical Sciences, Faculty of Medicine, University of Oslo, Sognsvannsveien 9, 0372 Oslo, Norway.

Department of Pharmacology and Toxicology, University of Toronto, 1 King's College Circle, Toronto, ON M5S 1A8, Canada.

出版信息

Cells. 2021 Mar 11;10(3):623. doi: 10.3390/cells10030623.

DOI:10.3390/cells10030623
PMID:33799807
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8001409/
Abstract

ADP-ribosylation is a post-translational protein modification catalyzed by a family of proteins known as poly-ADP-ribose polymerases. PARP7 (TIPARP; ARTD14) is a mono-ADP-ribosyltransferase involved in several cellular processes, including responses to hypoxia, innate immunity and regulation of nuclear receptors. Since previous studies suggested that PARP7 was regulated by 17β-estradiol, we investigated whether PARP7 regulates estrogen receptor α signaling. We confirmed the 17β-estradiol-dependent increases of PARP7 mRNA and protein levels in MCF-7 cells, and observed recruitment of estrogen receptor α to the promoter of PARP7. Overexpression of PARP7 decreased ligand-dependent estrogen receptor α signaling, while treatment of PARP7 knockout MCF-7 cells with 17β-estradiol resulted in increased expression of and recruitment to estrogen receptor α target genes, in addition to increased proliferation. Co-immunoprecipitation assays revealed that PARP7 mono-ADP-ribosylated estrogen receptor α, and mass spectrometry mapped the modified peptides to the receptor's ligand-independent transactivation domain. Co-immunoprecipitation with truncated estrogen receptor α variants identified that the hinge region of the receptor is required for PARP7-dependent mono-ADP-ribosylation. These results imply that PARP7-mediated mono-ADP-ribosylation may play an important role in estrogen receptor positive breast cancer.

摘要

ADP-核糖基化是一种翻译后蛋白质修饰，由一类称为多聚 ADP-核糖聚合酶的蛋白质催化。PARP7（TIPARP；ARTD14）是一种单 ADP-核糖基转移酶，参与多种细胞过程，包括对缺氧、先天免疫和核受体调节的反应。由于先前的研究表明 PARP7 受 17β-雌二醇调节，我们研究了 PARP7 是否调节雌激素受体 α 信号。我们证实了 MCF-7 细胞中 17β-雌二醇依赖性 PARP7 mRNA 和蛋白水平的增加，并观察到雌激素受体 α 募集到 PARP7 启动子。PARP7 的过表达降低了配体依赖性雌激素受体 α 信号，而用 17β-雌二醇处理 PARP7 敲除 MCF-7 细胞导致雌激素受体 α 靶基因的表达增加和募集，以及增殖增加。免疫共沉淀测定显示 PARP7 单 ADP-核糖基化了雌激素受体 α，而质谱将修饰肽映射到受体的配体非依赖性转录激活域。与截断的雌激素受体 α 变体的免疫共沉淀鉴定出受体的铰链区域是 PARP7 依赖性单 ADP-核糖基化所必需的。这些结果表明，PARP7 介导的单 ADP-核糖基化可能在雌激素受体阳性乳腺癌中发挥重要作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/365b8ee0f135/cells-10-00623-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/9a5451c72699/cells-10-00623-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/05bb815515d5/cells-10-00623-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/e73b87aa3461/cells-10-00623-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/e06d27526f3e/cells-10-00623-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/2c707382031b/cells-10-00623-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/ec9c3ee8b568/cells-10-00623-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/365b8ee0f135/cells-10-00623-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/9a5451c72699/cells-10-00623-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/05bb815515d5/cells-10-00623-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/e73b87aa3461/cells-10-00623-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/e06d27526f3e/cells-10-00623-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/2c707382031b/cells-10-00623-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/ec9c3ee8b568/cells-10-00623-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df8/8001409/365b8ee0f135/cells-10-00623-g007.jpg

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