IndraLab

Statements


| 7

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"Increasing evidence links deregulation of the ubiquitin specific proteases 22 (USP22) deubitiquitylase to cancer development and progression in a select group of tumor types, but its specificity and underlying mechanisms of action are not well defined."

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"Moreover, the study of the corresponding mechanism by which HULC upregulated COX-2 showed that HULC enhanced the level of ubiquitin specific peptidase 22 (USP22), which decreased ubiquitin mediated degradation of COX-2 protein by removing the conjugated polyubiquitin chains from COX-2 and finally stabilized COX2 protein."

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"It was also indicated that lncRNA HULC could up-regulate expression of ubiquitin-specific peptidase 22 (USP22) and reduce the ubiquitin-mediated degradation of Sirt1 protein by removing the conjugated polyubiquitin chain of Sirt1 [135]."

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"In liver cancer, upregulation of lncRNA HULC activates autophagy by increasing the expression of ubiquitin specific peptidase 22 (USP22) which in turn prevents the ubiquitin mediated degradation of silent information regulator 1 (SIRT1) by removing the conjugated polyubiquitin chains from SIRT1."

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"On the contrary, the deubiqutinase USP22 antagonizes the ubiquitin ligase complex RNF20/40 on H2B monoubiquitination."

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"It belongs to the DUB subset of Machado–Joseph disease (MJD) proteic domain-containing peptidases with Atxn3 (a.k.a. MJD1 and SCA3), encoded by the gene mutated in MJD, also termed type-3 spinocerebellar ataxia (SCA3), and Josephin domain-containing DUbs JosD1 and JosD2 (Table 1.7).27Aggregates formed by polyglutamine-expanded ataxin-7 sequester ubiquitin-specific peptidase USP22 that cannot then fulfill its deubiquitinating function in the SAGA complex, causing cytotoxicity and neurodegeneration [109]."
| PMC

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"HULC is overexpressed in HCC as it promotes growth in cancer cells through enhancing ubiquitin specific peptidase 22 (USP22) which reduces ubiquitin mediated degradation of COX-2 protein hence stabilizing and upregulating COX-2 protein [XREF_BIBR]."