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卵巢肿瘤B1介导的热休克转录因子1去泛素化对于子宫内膜异位症的糖酵解和发展至关重要。

Ovarian tumorB1-mediated heat shock transcription factor 1 deubiquitination is critical for glycolysis and development of endometriosis.

作者信息

Ling Xi, Lu Jiayi, Wang Xiaoyun, Liu Lan, Liu Lu, Wang Yadi, Sun Yujun, Ren Chune, Lu Chao, Yu Zhenhai

机构信息

Department of Reproductive Medicine, Affiliated Hospital of Weifang Medical University, Weifang 261000, China.

School of Clinical Medicine, Weifang Medical University, Weifang 261000, China.

出版信息

iScience. 2022 Oct 14;25(11):105363. doi: 10.1016/j.isci.2022.105363. eCollection 2022 Nov 18.

DOI:10.1016/j.isci.2022.105363
PMID:36339263
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9626688/
Abstract

Endometriosis is a common chronic condition characterized by abnormal growth of the endometrium outside the uterus. Heat shock transcription factor 1 (HSF1) is a significant regulator of the proteotoxic stress response and plays an essential role in developing endometriosis. However, the mechanisms regulating HSF1 protein stability in endometriosis remain unclear. Here, we demonstrate that OTUB1 interacts with HSF1 and promotes HSF1 protein stability through deubiquitination. In addition, OTUB1 enhances glycolysis and epithelial-mesenchymal transition of endometriosis cells, leading to promote proliferation, migration, and invasion of endometriosis cells. The progression of endometriosis is inhibited in an OTUB1-knockout mouse model. In summary, OTUB1 promotes the development of endometriosis by up-regulating HSF1. OTUB1/HSF1 axis may become a new therapeutic target for endometriosis.

摘要

子宫内膜异位症是一种常见的慢性疾病，其特征是子宫内膜在子宫外异常生长。热休克转录因子1（HSF1）是蛋白毒性应激反应的重要调节因子，在子宫内膜异位症的发生发展中起重要作用。然而，子宫内膜异位症中调节HSF1蛋白稳定性的机制仍不清楚。在此，我们证明OTUB1与HSF1相互作用，并通过去泛素化促进HSF1蛋白稳定性。此外，OTUB1增强子宫内膜异位症细胞的糖酵解和上皮-间质转化，从而促进子宫内膜异位症细胞的增殖、迁移和侵袭。在OTUB1基因敲除小鼠模型中，子宫内膜异位症的进展受到抑制。总之，OTUB1通过上调HSF1促进子宫内膜异位症的发展。OTUB1/HSF1轴可能成为子宫内膜异位症的一个新的治疗靶点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/b198e2e984e1/gr8.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/ee54f8b6914c/gr3.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/e5ee5c8bcfbf/gr5.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/9f5936e8c221/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/b198e2e984e1/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/09a42b866a62/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/da7f0aade0e0/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/a1a03ddb2ac0/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/ee54f8b6914c/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/2ef80c3e8a22/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/e5ee5c8bcfbf/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/e0139f93cce2/gr6.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ead/9626688/b198e2e984e1/gr8.jpg

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