SUMOylation of PES1 upregulates its stability and function via inhibiting its ubiquitination

Li, Shujing; Wang, Miao; Qu, Xiaoni; Xu, Zhaowei; Yang, Yangyang; Su, Qiming; Wu, Harry X.

doi:10.18632/oncotarget.10494

Cited by 27 publications

(18 citation statements)

References 28 publications

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“…HEK293T, COS-7, HeLa, and MDA-MB-231 cells were used in our previous studies 37 , 55 , 56 . ZR-75-1, MCF-7, T47D, and SK-BR-3 cells were kindly provided by Dr Wei Cheng of Dalian Medical University.…”

Section: Methodsmentioning

confidence: 99%

Checkpoint suppressor 1 suppresses transcriptional activity of ERα and breast cancer cell proliferation via deacetylase SIRT1

Yang

et al. 2018

Cell Death Dis

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Breast cancer is a highly heterogeneous carcinoma in women worldwide, but the underlying mechanisms that account for breast cancer initiation and development have not been fully established. Mounting evidence indicates that Checkpoint suppressor 1 (CHES1) is tightly associated with tumorigenesis and prognosis in many types of cancer. However, the definitive function of CHES1 in breast cancer remains to be explored. Here we showed that CHES1 had a physical interaction with estrogen receptor-α (ERα) and repressed the transactivation of ERα in breast cancer cells. Mechanistically, the interaction between CHES1 and ERα enhanced the recruitment of nicotinamide adenine dinucleotide (NAD+) deacetylase Sirtuin 1 (SIRT1), and it further induced SIRT1-mediated ERα deacetylation and repression on the promoter-binding enrichment of ERα. In addition, we also found that the expression of CHES1 was repressed by estrogen-ERα signaling and the expression level of CHES1 was significantly downregulated in ERα-positive breast cancer. The detailed mechanism was that ERα may directly bind to CHES1 potential promoter via recognizing the conserved estrogen response element (ERE) motif in response to estrogen stimulation. Functionally, CHES1 inhibited ERα-mediated proliferation and tumorigenesis of breast cancer cells in vivo and in vitro. Totally, these results identified a negative cross-regulatory loop between ERα and CHES1 that was required for growth of breast cancer cells, it might uncover novel insight into molecular mechanism of CHES1 involved in breast cancer and provide new avenues for molecular-targeted therapy in hormone-regulated breast cancer.

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Section: Methodsmentioning

confidence: 99%

Checkpoint suppressor 1 suppresses transcriptional activity of ERα and breast cancer cell proliferation via deacetylase SIRT1

Yang

et al. 2018

Cell Death Dis

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“…SUMOylation can stabilize PES1 by inhibiting its ubiquitination, which is stimulated by estrogen ( 83 ). PES1 is a component of the PeBoW complex which is required for the formation of the 60S ribosomal subunits.…”

Section: Sumo and Cancermentioning

confidence: 99%

The post-translational modification, SUMOylation, and cancer (Review)

et al. 2018

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SUMOylation is a reversible post-translational modification which has emerged as a crucial molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune responses, carcinogenesis, cell cycle progression and apoptosis. Four SUMO isoforms have been identified, which are SUMO1, SUMO2/3 and SUMO4. The small ubiquitin-like modifier (SUMO) pathway is conserved in all eukaryotes and plays pivotal roles in the regulation of gene expression, cellular signaling and the maintenance of genomic integrity. The SUMO catalytic cycle includes maturation, activation, conjugation, ligation and de-modification. The dysregulation of the SUMO system is associated with a number of diseases, particularly cancer. SUMOylation is widely involved in carcinogenesis, DNA damage response, cancer cell proliferation, metastasis and apoptosis. SUMO can be used as a potential therapeutic target for cancer. In this review, we briefly outline the basic concepts of the SUMO system and summarize the involvement of SUMO proteins in cancer cells in order to better understand the role of SUMO in human disease.

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“…The SUMOylation of HTT-fragment increases neurodegeneration, whereas its ubiquitination decreases neurodegeneration in a Huntington's disease model [ 32 ]. PES1 is a component of the PeBoW complex; when stimulated by oestrogen, the SUMOylation of PES1 upregulates its stability and function via inhibiting its ubiquitination [ 33 ]. Post-translational modification of proliferating cell nuclear antigen PCNA can be modified by ubiquitin and SUMO in response to DNA damage [ 34 ].…”

Section: Signal Crosstalk Of Sumoylation With Ubiquitinationmentioning

confidence: 99%

Protein SUMOylation modification and its associations with disease

et al. 2017

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SUMOylation, as a post-translational modification, plays essential roles in various biological functions including cell growth, migration, cellular responses to stress and tumorigenesis. The imbalance of SUMOylation and deSUMOylation has been associated with the occurrence and progression of various diseases. Herein, we summarize and discuss the signal crosstalk between SUMOylation and ubiquitination of proteins, protein SUMOylation relations with several diseases, and the identification approaches for SUMOylation site. With the continuous development of bioinformatics and mass spectrometry, several accurate and high-throughput methods have been implemented to explore small ubiquitin-like modifier-modified substrates and sites, which is helpful for deciphering protein SUMOylation-mediated molecular mechanisms of disease.

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SUMOylation of PES1 upregulates its stability and function via inhibiting its ubiquitination

Cited by 27 publications

References 28 publications

Checkpoint suppressor 1 suppresses transcriptional activity of ERα and breast cancer cell proliferation via deacetylase SIRT1

Checkpoint suppressor 1 suppresses transcriptional activity of ERα and breast cancer cell proliferation via deacetylase SIRT1

The post-translational modification, SUMOylation, and cancer (Review)

Protein SUMOylation modification and its associations with disease

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