USP22 acts as an oncogene by regulating the stability of cyclooxygenase-2 in non-small cell lung cancer

Xiao, Haibo; Tian, Yuan; Yang, Yang; Hu, Fengqing; Xie, Xian-Jin; Mei, Ju; Ding, Fang

doi:10.1016/j.bbrc.2015.03.093

Cited by 31 publications

(26 citation statements)

References 27 publications

(31 reference statements)

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“…Non-histone substrates identified so far include the telomeric repeat binding factor 1 (TRF1) [29], sirtuin 1 (SIRT1) [30, 31], cyclin B1 [32], the far upstream element -FUSE- binding protein 1 (FBP1) [33], hairy and enhancer of split 1 (Hes1) [34], regulator of calcineurin 1 (RCAN1) [35], nuclear factor of activated T-cells (NFAT) [36], cyclooxygenase 2 (COX-2) [37] and sucrose-nonfermenting 1 (Snf1) [38]. …”

Section: Usp22 Structure and Saga Deubiquitylase Module Formationmentioning

confidence: 99%

Ubiquitin-specific peptidase 22 functions and its involvement in disease

Melo‐Cardenas

Zhang

et al. 2016

Oncotarget

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Deubiquitylases remove ubiquitin moieties from different substrates to regulate protein activity and cell homeostasis. Since this posttranslational modification plays a role in several different cellular functions, its deregulation has been associated with different pathologies. Aberrant expression of the Ubiquitin-Specific Peptidase 22 (USP22) has been associated with poor cancer prognosis and neurological disorders. However, little is known about USP22 role in these pathologies or in normal physiology. This review summarizes the current knowledge about USP22 function from yeast to human and provides an overview of the possible mechanisms by which USP22 is emerging as a potential oncogene.

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Section: Usp22 Structure and Saga Deubiquitylase Module Formationmentioning

confidence: 99%

Ubiquitin-specific peptidase 22 functions and its involvement in disease

Melo‐Cardenas

Zhang

et al. 2016

Oncotarget

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“…Ubiquitin-specific Protease 22 (USP22) is the deubiquitinating subunit of the SAGA mDUB complex [ 10 ] and has been reported to affect transcription by the deubiquitination of histones H2A and H2B [ 11 – 14 ]. Additionally, USP22 functions to stabilize specific proteins via the removal of ubiquitin moieties, thereby preventing proteasomal degradation [ 15 – 25 ]. Notably, in addition to H2B, the histone deacetylase Sirt1 has been reported to be a central deubiquitination target of USP22 [ 22 ].…”

Section: Introductionmentioning

confidence: 99%

Usp22 deficiency impairs intestinal epithelial lineage specification in vivo

et al. 2015

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Epigenetic regulatory mechanisms play a central role in controlling gene expression during development, cell differentiation and tumorigenesis. Monoubiquitination of histone H2B is one epigenetic modification which is dynamically regulated by the opposing activities of specific ubiquitin ligases and deubiquitinating enzymes (DUBs). The Ubiquitin-specific Protease 22 (USP22) is the ubiquitin hydrolase component of the human SAGA complex which deubiquitinates histone H2B during transcription. Recently, many studies have investigated an oncogenic potential of USP22 overexpression. However, its physiological function in organ maintenance, development and its cellular function remain largely unknown. A previous study reported embryonic lethality in Usp22 knockout mice. Here we describe a mouse model with a global reduction of USP22 levels which expresses the LacZ gene under the control of the endogenous Usp22 promoter. Using this reporter we found Usp22 to be ubiquitously expressed in murine embryos. Notably, adult Usp22lacZ/lacZ displayed low residual Usp22 expression levels coupled with a reduced body size and weight. Interestingly, the reduction of Usp22 significantly influenced the frequency of differentiated cells in the small intestine and the brain while H2B and H2Bub1 levels remained constant. Taken together, we provide evidence for a physiological role for USP22 in controlling cell differentiation and lineage specification.

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“…USP22 is a biomarker for advanced malignancy in numerous tumor types, including non-small cell lung cancer [33], gastric carcinoma [34] and hepatocellular cancer [35]. We detected simultaneous overexpression of USP22 and AP4 in CRC primary carcinoma.…”

Section: Discussionmentioning

confidence: 94%

USP22 drives colorectal cancer invasion and metastasis via epithelial-mesenchymal transition by activating AP4

Yang

et al. 2017

Oncotarget

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Ubiquitin specific peptidase 22 (USP22), a putative cancer stem cell marker, is overexpressed in liver metastases of colorectal cancer (CRC). However, the mechanism by which USP22 promotes CRC metastasis remains largely unknown. Here, we report that USP22 and AP4 are simultaneously overexpressed during TGF-β1-induced CRC cell epithelial-mesenchymal transition (EMT). USP22 up-regulation enhances CRC cell migration and invasion and EMT-related marker and AP4 expression, but these effects are partly blocked by AP4 knockdown. In addition, USP22 binds to the promoter region of AP4 to activate its transcription. In vivo, elevated USP22 expression promotes CRC cell metastasis to the lungs in nude mice, as evidenced by the fact that CRC metastatic nodules stain deeply positive for USP22 and AP4. In human CRC tissues, the genes encoding USP22 and AP4 are overexpressed in metastatic liver lesions compared with primary cancer tissues, and their overexpression is significantly associated with poor CRC patient survival. These findings indicate that USP22 and AP4 may serve as prognostic markers for predicting the risk of developing distant metastases in CRC.

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USP22 acts as an oncogene by regulating the stability of cyclooxygenase-2 in non-small cell lung cancer

Cited by 31 publications

References 27 publications

Ubiquitin-specific peptidase 22 functions and its involvement in disease

Ubiquitin-specific peptidase 22 functions and its involvement in disease

Usp22 deficiency impairs intestinal epithelial lineage specification in vivo

USP22 drives colorectal cancer invasion and metastasis via epithelial-mesenchymal transition by activating AP4

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