TRIM32/USP11 Balances ARID1A Stability and the Oncogenic/Tumor-Suppressive Status of Squamous Cell Carcinoma

Luo, Qingyu; Wu, Xiaowei; Nan, Yabing; Chang, Wan; Zhao, Pengfei; Zhang, Yiping; Su, Dan; Liu, Zhihua

doi:10.1016/j.celrep.2019.12.017

Cited by 40 publications

(35 citation statements)

References 55 publications

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“…Nevertheless, SCCs are characterized by low ARID1A protein expression, indicating that the TRIM32-dependent degradation of ARID1A may represent a relevant mechanism contributing to underexpress this epigenetic factor in SCC. Notably, TRIM32 action is counteracted by the DUB USP11, which promotes the stabilization of ARID1A protein [57]. Consistently, SCC samples show a negative correlation between TRIM32 and ARID1A expression and a positive correlation between USP11 and ARID1A expression.…”

Section: Additional E3s Involved In Sccsmentioning

confidence: 65%

“…Human HNSCC samples also display an elevated level of TRIM32 [54]. Although different TRIM32 substrates underlying its pro-oncogenic function have been identified, a recent report uncovered a novel oncogenic route exploited by TRIM32 in SCCs [57]. Luo et al reported that TRIM32 is able to target the SWI/SNF complex subunit ARID1A, a potential tumor suppressor.…”

Section: Additional E3s Involved In Sccsmentioning

confidence: 99%

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The Impact of the Ubiquitin System in the Pathogenesis of Squamous Cell Carcinomas

Gatti

Bernassola

Talora

et al. 2020

Cancers

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The ubiquitin system is a dynamic regulatory pathway controlling the activity, subcellular localization and stability of a myriad of cellular proteins, which in turn affects cellular homeostasis through the regulation of a variety of signaling cascades. Aberrant activity of key components of the ubiquitin system has been functionally linked with numerous human diseases including the initiation and progression of human tumors. In this review, we will contextualize the importance of the two main components of the ubiquitin system, the E3 ubiquitin ligases (E3s) and deubiquitinating enzymes (DUBs), in the etiology of squamous cell carcinomas (SCCs). We will discuss the signaling pathways regulated by these enzymes, emphasizing the genetic and molecular determinants underlying their deregulation in SCCs.

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Section: Additional E3s Involved In Sccsmentioning

confidence: 65%

Section: Additional E3s Involved In Sccsmentioning

confidence: 99%

The Impact of the Ubiquitin System in the Pathogenesis of Squamous Cell Carcinomas

Gatti

Bernassola

Talora

et al. 2020

Cancers

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“…Based on our observation that SPRTN and USP11 interact (Figure 1 and 2) and because USP11 is a deubiquitinase (Luo et al, 2020, Deng et al, 2018, Orthwein et al, 2015, we investigated whether SPRTN is a substrate for USP11 deubiquitinase. Indeed, we found that overexpression of Myc-USP11 FL, but not C318S catalytic inactive mutant was able to deubiquitinate SFB-SPRTN in HEK 293T cells ( Figure 3A).…”

Section: Usp11 Deubiquitinates Sprtn In Cells and In Vitromentioning

confidence: 99%

“…USP11 (Ubiquitin carboxyl-terminal hydrolase or ubiquitin specific protease 11) belongs to the ubiquitin specific protease (USP or UBP) family of DUBs. USP11 participates in processes such as TGFβ signaling, pro-inflammatory signaling, viral replication and NF-κB signaling by regulating the protein stability of various targets such as ARID1A, TβRII, CDKN2A, RAE1, XIAP, HPV16-E7 and IκBα (Luo et al, 2020, Deng et al, 2018, Jacko et al, 2016, Lin et al, 2008, Sun et al, 2010, Stockum et al, 2018. USP11 also functions in DSB repair, wherein USP11 deubiquitinates H2AX to regulate the recruitment of RAD51 and 53BP1 to damage foci (Ting et al, 2019, Yu et al, 2016.…”

Section: Introductionmentioning

confidence: 99%

USP11 deubiquitinates monoubiquitinated SPRTN to repair DNA-protein crosslinks

Perry

Kollala

Biegert

et al. 2020

Preprint

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SUMMARYDNA-protein crosslinks (DPCs) are toxic DNA lesions that interfere with DNA metabolic processes such as replication, transcription and recombination. SPRTN is a replication-coupled DNA-dependent metalloprotease that cleaves proteins crosslinked to DNA to promote DPC repair. SPRTN function is tightly regulated by a monoubiquitin switch that controls SPRTN chromatin accessibility during DPC repair. The deubiquitinase regulating SPRTN function in DPC repair is unknown. Here, we identify USP11 as a SPRTN deubiquitinase. USP11 interacts with SPRTN and cleaves monoubiquitinated SPRTN in cells and in vitro. USP11 depletion impairs SPRTN deubiquitination in response to formaldehyde-induced DPCs. Loss of USP11 causes an accumulation of unrepaired DPCs and cellular hypersensitivity to treatment with DPC-inducing agents. Our findings elucidate the function of USP11 in the regulation of SPRTN monoubiquitination and SPRTN-mediated DPC repair.

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“…Ubiquitin‐specific protease 11 (USP11) is a member of the USP subfamily of DUBs, which has been implicated in the regulation of various cellular functions by controlling its substrates’ stability 7 . Likewise, USP11 malfunction has been found in many types of cancer and related in tumour development and progression 8‐10 . In melanoma, overexpression of USP11 has been frequently observed and is correlated with poor prognosis 11 …”

Section: Introductionmentioning

confidence: 99%

The regulation of NONO by USP11 via deubiquitination is linked to the proliferation of melanoma cells

Feng

Dai

et al. 2020

J Cellular Molecular Medi

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Ubiquitin‐specific protease 11 (USP11) has been implicated in the regulation of DNA repair, apoptosis, signal transduction and cell cycle. It belongs to a USP subfamily of deubiquitinases. Although previous research has shown that USP11 overexpression is frequently found in melanoma and is correlated with a poor prognosis, the potential molecular mechanism of USP11 in melanoma remains indefinitive. Here, we report that USP11 and NONO colocalize and interact with each other in the nucleus of melanoma cells. As a result, the knockdown of USP11 decreases NONO levels. Whereas, overexpression of USP11 increases NONO levels in a dose‐dependent manner. Furthermore, we reveal that USP11 protects NONO protein from proteasome‐mediated degradation by removing poly‐ubiquitin chains conjugated onto NONO. Functionally, USP11 mediated melanoma cell proliferation via the regulation of NONO levels because ablation of USP11 inhibits the proliferation which could be rescued by ectopic expression of NONO protein. Moreover, a significant positive correlation between USP11 and NONO concentrations was found in clinical melanoma samples. Collectively, these results demonstrate that USP11 is a new deubiquitinase of NONO and that the signalling axis of USP11‐NONO is significantly involved in melanoma proliferation.

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TRIM32/USP11 Balances ARID1A Stability and the Oncogenic/Tumor-Suppressive Status of Squamous Cell Carcinoma

Cited by 40 publications

References 55 publications

The Impact of the Ubiquitin System in the Pathogenesis of Squamous Cell Carcinomas

The Impact of the Ubiquitin System in the Pathogenesis of Squamous Cell Carcinomas

USP11 deubiquitinates monoubiquitinated SPRTN to repair DNA-protein crosslinks

The regulation of NONO by USP11 via deubiquitination is linked to the proliferation of melanoma cells

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