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Article: Targeting the MYC Ubiquitination-Proteasome Degradation Pathway for Cancer Therapy.

Sun, Xiao-Xin / Li, Yanping / Sears, Rosalie C / Dai, Mu-Shui

2021 Volume 11, Page(s) 679445

Abstract: Deregulated MYC overexpression and activation contributes to tumor growth and progression. Given the short half-life and unstable nature of the MYC protein, it is not surprising that the oncoprotein is highly ... ...

Abstract	Deregulated MYC overexpression and activation contributes to tumor growth and progression. Given the short half-life and unstable nature of the MYC protein, it is not surprising that the oncoprotein is highly regulated
Language	English
Publishing date	2021-06-11
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2021.679445
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Article ; Online: p73 to the rescue: Role of RPL26.

Sun, Xiao-Xin / Dai, Mu-Shui

Oncotarget

2017 Volume 8, Issue 4, Page(s) 5641–5642

Language	English
Publishing date	2017-03-16
Publishing country	United States
Document type	News
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.14383
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Article ; Online: The Ubiquitin-specific Protease USP36 Associates with the Microprocessor Complex and Regulates miRNA Biogenesis by SUMOylating DGCR8.

Li, Yanping / Carey, Timothy S / Feng, Catherine H / Zhu, Hong-Ming / Sun, Xiao-Xin / Dai, Mu-Shui

Cancer research communications

2023 Volume 3, Issue 3, Page(s) 459–470

Abstract: miRNA biogenesis is a cellular process that produces mature miRNAs from their primary transcripts, pri-miRNAs, via two RNAse III enzyme complexes: the Drosha-DGCR8 microprocessor complex in the nucleus and the Dicer-TRBP complex in the cytoplasm. ... ...

Abstract	miRNA biogenesis is a cellular process that produces mature miRNAs from their primary transcripts, pri-miRNAs, via two RNAse III enzyme complexes: the Drosha-DGCR8 microprocessor complex in the nucleus and the Dicer-TRBP complex in the cytoplasm. Emerging evidence suggests that miRNA biogenesis is tightly regulated by posttranscriptional and posttranslational modifications and aberrant miRNA biogenesis is associated with various human diseases including cancer. DGCR8 has been shown to be modified by SUMOylation. Yet, the SUMO ligase mediating DGCR8 SUMOylation is currently unknown. Here, we report that USP36, a nucleolar ubiquitin-specific protease essential for ribosome biogenesis, is a novel regulator of DGCR8. USP36 interacts with the microprocessor complex and promotes DGCR8 SUMOylation, specifically modified by SUMO2. USP36-mediated SUMOylation does not affect the levels of DGCR8 and the formation of the Drosha-DGCR8 complex, but promotes the binding of DGCR8 to pri-miRNAs. Consistently, abolishing DGCR8 SUMOylation significantly attenuates its binding to pri-miRNAs and knockdown of USP36 attenuates pri-miRNA processing, resulting in marked reduction of tested mature miRNAs. Induced expression of a SUMOylation-defective mutant of DGCR8 inhibits cell proliferation. Together, these results suggest that USP36 plays an important role in regulating miRNA biogenesis by SUMOylating DGCR8. Significance: This study identifies that USP36 mediates DGCR8 SUMOylation by SUMO2 and is critical for miRNA biogenesis. As USP36 is frequently overexpressed in various human cancers, our study suggests that deregulated USP36-miRNA biogenesis pathway may contribute to tumorigenesis.
MeSH term(s)	Humans ; MicroRNAs/genetics ; RNA-Binding Proteins/genetics ; RNA Processing, Post-Transcriptional ; Carcinogenesis/genetics ; Neoplasms/genetics ; Microcomputers ; Ubiquitin Thiolesterase/genetics
Chemical Substances	MicroRNAs ; RNA-Binding Proteins ; DGCR8 protein, human ; USP36 protein, human ; Ubiquitin Thiolesterase (EC 3.4.19.12)
Language	English
Publishing date	2023-03-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2767-9764
ISSN (online)	2767-9764
DOI	10.1158/2767-9764.CRC-22-0344
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Article: Molecular Crosstalk Between MYC and HIF in Cancer.

Li, Yanping / Sun, Xiao-Xin / Qian, David Z / Dai, Mu-Shui

Frontiers in cell and developmental biology

2020 Volume 8, Page(s) 590576

Abstract: The transcription factor c-MYC (MYC thereafter) is a global regulator of gene expression. It is overexpressed or deregulated in human cancers of diverse origins and plays a key role in the development of cancers. Hypoxia-inducible factors (HIFs), a ... ...

Abstract	The transcription factor c-MYC (MYC thereafter) is a global regulator of gene expression. It is overexpressed or deregulated in human cancers of diverse origins and plays a key role in the development of cancers. Hypoxia-inducible factors (HIFs), a central regulator for cells to adapt to low cellular oxygen levels, is also often overexpressed and activated in many human cancers. HIF mediates the primary transcriptional response of a wide range of genes in response to hypoxia. Earlier studies focused on the inhibition of MYC by HIF during hypoxia, when MYC is expressed at physiological level, to help cells survive under low oxygen conditions. Emerging evidence suggests that MYC and HIF also cooperate to promote cancer cell growth and progression. This review will summarize the current understanding of the complex molecular interplay between MYC and HIF.
Language	English
Publishing date	2020-11-05
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2020.590576
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Article ; Online: Detection of Post-translational Modifications on MYC.

Daniel, Colin J / Sun, Xiao-Xin / Chen, Yingxiao / Zhang, Xiaoli / Dai, Mu-Shui / Sears, Rosalie C

Methods in molecular biology (Clifton, N.J.)

2021 Volume 2318, Page(s) 69–85

Abstract: Detection of post-translational modifications in c-Myc is an invaluable tool in assessing Myc status, particularly in cancer. However, it can be challenging to detect these modifications. The evaluation of phosphorylation status of c-Myc can also be ... ...

Abstract	Detection of post-translational modifications in c-Myc is an invaluable tool in assessing Myc status, particularly in cancer. However, it can be challenging to detect these modifications. The evaluation of phosphorylation status of c-Myc can also be challenging with the current commercially available phosphorylation sensitive antibodies. Here, we describe protocols for the immunoprecipitation of endogenous c-Myc to probe for phosphorylation status, as well as the detection of ubiquitination and SUMOylation on c-Myc. We will also discuss the challenges of detecting phosphorylated c-Myc in formalin-fixed paraffin-embedded tissues by immunofluorescence and describe a protocol using a new rat monoclonal antibody we have generated suitable for this purpose.
MeSH term(s)	Fluorescent Antibody Technique ; Genes, myc/genetics ; Genes, myc/physiology ; Humans ; Immunoprecipitation/methods ; Phosphorylation ; Protein Processing, Post-Translational/genetics ; Protein Processing, Post-Translational/physiology ; Proteins/genetics ; Proteins/metabolism ; Proto-Oncogene Proteins c-myc/genetics ; Proto-Oncogene Proteins c-myc/metabolism ; Sumoylation ; Ubiquitination
Chemical Substances	Proteins ; Proto-Oncogene Proteins c-myc
Language	English
Publishing date	2021-05-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1476-1_5
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Article ; Online: Molecular Crosstalk Between MYC and HIF in Cancer

Yanping Li / Xiao-Xin Sun / David Z. Qian / Mu-Shui Dai

Frontiers in Cell and Developmental Biology, Vol

2020 Volume 8

Abstract	The transcription factor c-MYC (MYC thereafter) is a global regulator of gene expression. It is overexpressed or deregulated in human cancers of diverse origins and plays a key role in the development of cancers. Hypoxia-inducible factors (HIFs), a central regulator for cells to adapt to low cellular oxygen levels, is also often overexpressed and activated in many human cancers. HIF mediates the primary transcriptional response of a wide range of genes in response to hypoxia. Earlier studies focused on the inhibition of MYC by HIF during hypoxia, when MYC is expressed at physiological level, to help cells survive under low oxygen conditions. Emerging evidence suggests that MYC and HIF also cooperate to promote cancer cell growth and progression. This review will summarize the current understanding of the complex molecular interplay between MYC and HIF.
Keywords	MYC ; HIF1α ; HIF2α ; transcription ; protein stability ; metabolism ; Biology (General) ; QH301-705.5
Subject code	500 ; 610
Language	English
Publishing date	2020-11-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
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Article ; Online: The ubiquitin-specific protease USP36 SUMOylates EXOSC10 and promotes the nucleolar RNA exosome function in rRNA processing.

Chen, Yingxiao / Li, Yanping / Dai, Roselyn S / Savage, Jonathan C / Shinde, Ujwal / Klimek, John / David, Larry L / Young, Emma A / Hafner, Markus / Sears, Rosalie C / Sun, Xiao-Xin / Dai, Mu-Shui

Nucleic acids research

2023 Volume 51, Issue 8, Page(s) 3934–3949

Abstract: The RNA exosome is an essential 3' to 5' exoribonuclease complex that mediates degradation, processing and quality control of virtually all eukaryotic RNAs. The nucleolar RNA exosome, consisting of a nine-subunit core and a distributive 3' to 5' ... ...

Abstract	The RNA exosome is an essential 3' to 5' exoribonuclease complex that mediates degradation, processing and quality control of virtually all eukaryotic RNAs. The nucleolar RNA exosome, consisting of a nine-subunit core and a distributive 3' to 5' exonuclease EXOSC10, plays a critical role in processing and degrading nucleolar RNAs, including pre-rRNA. However, how the RNA exosome is regulated in the nucleolus is poorly understood. Here, we report that the nucleolar ubiquitin-specific protease USP36 is a novel regulator of the nucleolar RNA exosome. USP36 binds to the RNA exosome through direct interaction with EXOSC10 in the nucleolus. Interestingly, USP36 does not significantly regulate the levels of EXOSC10 and other tested exosome subunits. Instead, it mediates EXOSC10 SUMOylation at lysine (K) 583. Mutating K583 impaired the binding of EXOSC10 to pre-rRNAs, and the K583R mutant failed to rescue the defects in rRNA processing and cell growth inhibition caused by knockdown of endogenous EXOSC10. Furthermore, EXOSC10 SUMOylation is markedly reduced in cells in response to perturbation of ribosomal biogenesis. Together, these results suggest that USP36 acts as a SUMO ligase to promote EXOSC10 SUMOylation critical for the RNA exosome function in ribosome biogenesis.
MeSH term(s)	Cell Nucleolus/genetics ; Cell Nucleolus/metabolism ; Exoribonucleases/genetics ; Exoribonucleases/metabolism ; Exosome Multienzyme Ribonuclease Complex/genetics ; Exosome Multienzyme Ribonuclease Complex/metabolism ; RNA/metabolism ; RNA Precursors/genetics ; RNA Precursors/metabolism ; RNA Processing, Post-Transcriptional ; RNA, Ribosomal/genetics ; RNA, Ribosomal/metabolism ; Humans ; Cell Line
Chemical Substances	Exoribonucleases (EC 3.1.-) ; Exosome Multienzyme Ribonuclease Complex (EC 3.1.-) ; RNA (63231-63-0) ; RNA Precursors ; RNA, Ribosomal
Language	English
Publishing date	2023-03-13
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkad140
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Article ; Online: Writing and erasing MYC ubiquitination and SUMOylation.

Chen, Yingxiao / Sun, Xiao-Xin / Sears, Rosalie C / Dai, Mu-Shui

Genes & diseases

2019 Volume 6, Issue 4, Page(s) 359–371

Abstract: The transcription factor c-MYC (MYC thereafter) controls diverse transcription programs and plays a key role in the development of many human cancers. Cells develop multiple mechanisms to ensure that MYC levels and activity are precisely controlled in ... ...

Abstract	The transcription factor c-MYC (MYC thereafter) controls diverse transcription programs and plays a key role in the development of many human cancers. Cells develop multiple mechanisms to ensure that MYC levels and activity are precisely controlled in normal physiological context. As a short half-lived protein, MYC protein levels are tightly regulated by the ubiquitin proteasome system. Over a dozen of ubiquitin ligases have been found to ubiquitinate MYC whereas a number of deubiquitinating enzymes counteract this process. Recent studies show that SUMOylation and deSUMOylation can also regulate MYC protein stability and activity. Interestingly, evidence suggests an intriguing crosstalk between MYC ubiquitination and SUMOylation. Deregulation of the MYC ubiquitination-SUMOylation regulatory network may contribute to tumorigenesis. This review is intended to provide the current understanding of the complex regulation of the MYC biology by dynamic ubiquitination and SUMOylation and their crosstalk.
Language	English
Publishing date	2019-07-24
Publishing country	China
Document type	Journal Article ; Review
ZDB-ID	2821806-1
ISSN	2352-3042 ; 2352-3042
ISSN (online)	2352-3042
ISSN	2352-3042
DOI	10.1016/j.gendis.2019.05.006
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Article ; Online: The SUMO-specific protease SENP1 deSUMOylates p53 and regulates its activity.

Chauhan, Krishna M / Chen, Yingxiao / Chen, Yiyi / Liu, Andrew T / Sun, Xiao-Xin / Dai, Mu-Shui

Journal of cellular biochemistry

2020 Volume 122, Issue 2, Page(s) 189–197

Abstract: The stability and activity of the p53 tumor suppressor protein are tightly regulated by various posttranslational modifications, including SUMOylation. p53 can be modified by both SUMO1 and SUMO2, although how SUMOylation regulates p53 activity is still ... ...

Abstract	The stability and activity of the p53 tumor suppressor protein are tightly regulated by various posttranslational modifications, including SUMOylation. p53 can be modified by both SUMO1 and SUMO2, although how SUMOylation regulates p53 activity is still obscure. Whether p53 activity is directly regulated by deSUMOylation is also unclear. Here, we show that SENP1, a SUMO-specific protease implicated in pro-oncogenic roles, is a p53 deSUMOylating enzyme. SENP1 interacts with p53 and deSUMOylates p53 in cells and in vitro. Knockdown of SENP1 markedly induced p53 transactivation activity. We further show that SENP1 depletion synergizes with DNA damage-inducing agent etoposide to induce p53 activation and the expression of p21, leading to synergistic growth inhibition of cancer cells. Our results reveal that SENP1 is a critical p53 deSUMOylating enzyme and a promising therapeutic target in wild-type p53 containing cancer cells.
MeSH term(s)	Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; DNA Damage/drug effects ; DNA Damage/genetics ; Etoposide/pharmacology ; Humans ; Protein Processing, Post-Translational/drug effects ; Protein Processing, Post-Translational/genetics ; SUMO-1 Protein/genetics ; SUMO-1 Protein/metabolism ; Small Ubiquitin-Related Modifier Proteins/genetics ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	SUMO-1 Protein ; SUMO2 protein, human ; Small Ubiquitin-Related Modifier Proteins ; Tumor Suppressor Protein p53 ; Etoposide (6PLQ3CP4P3) ; SENP1 protein, human (EC 3.4.-) ; Cysteine Endopeptidases (EC 3.4.22.-)
Language	English
Publishing date	2020-08-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.29838
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Zs.A 1114: Show issues

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Jg. 1995 - 2021: Lesesall (1.OG)
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Article: Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1.

Sun, Xiao-Xin / Dai, Mu-Shui

World journal of biological chemistry

2014 Volume 5, Issue 2, Page(s) 75–84

Abstract: Deubiquitination has emerged as an important mechanism of p53 regulation. A number of deubiquitinating enzymes (DUBs) from the ubiquitin-specific protease family have been shown to regulate the p53-MDM2-MDMX networks. We recently reported that Otub1, a ... ...

Abstract	Deubiquitination has emerged as an important mechanism of p53 regulation. A number of deubiquitinating enzymes (DUBs) from the ubiquitin-specific protease family have been shown to regulate the p53-MDM2-MDMX networks. We recently reported that Otub1, a DUB from the OTU-domain containing protease family, is a novel p53 regulator. Interestingly, Otub1 abrogates p53 ubiquitination and stabilizes and activates p53 in cells independently of its deubiquitinating enzyme activity. Instead, it does so by inhibiting the MDM2 cognate ubiquitin-conjugating enzyme (E2) UbcH5. Otub1 also regulates other biological signaling through this non-canonical mechanism, suppression of E2, including the inhibition of DNA-damage-induced chromatin ubiquitination. Thus, Otub1 evolves as a unique DUB that mainly suppresses E2 to regulate substrates. Here we review the current progress made towards the understanding of the complex regulation of the p53 tumor suppressor pathway by DUBs, the biological function of Otub1 including its positive regulation of p53, and the mechanistic insights into how Otub1 suppresses E2.
Language	English
Publishing date	2014-01-15
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2564793-3
ISSN	1949-8454
ISSN	1949-8454
DOI	10.4331/wjbc.v5.i2.75
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