USP11 (C_term)
- Known as:
- USP11 (C_term)
- Catalog number:
- AP12023PU-N
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- USP11 (C_term)
Related genes to: USP11 (C_term)
- Gene:
- USP11 NIH gene
- Name:
- ubiquitin specific peptidase 11
- Previous symbol:
- -
- Synonyms:
- UHX1
- Chromosome:
- Xp11.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-01
- Date modifiied:
- 2016-10-05
Related products to: USP11 (C_term)
Related articles to: USP11 (C_term)
- An accumulation of evidence underscores the critical importance of both hypoxia and the immune microenvironment in driving the progression of osteosarcoma. Despite advancements in therapeutic strategies, osteosarcoma continues to pose a formidable challenge due to its aggressive nature and high metastatic potential. Nonetheless, the identification of reliable gene signatures that combine information on hypoxia and immune status to predict osteosarcoma prognosis remains an unmet need. - Source: PubMed
Publication date: 2026/06/20
Xie ShangfangYu WenyaoLin RunyeXin Songjian - Pathological cardiac hypertrophy is a key precursor to heart failure. Protein ubiquitination and deubiquitination are crucial mechanisms controlling cardiomyocyte signaling homeostasis. USP11, a ubiquitin-specific protease, has been implicated in multiple cellular regulatory processes, but its cardiac function remains unknown. Here, we investigated whether USP11 modulates cardiac hypertrophy and explored its downstream molecular mechanisms. - Source: PubMed
Publication date: 2026/06/18
Wang XijiaZong WenzheZhou DiJi XiaoyangAn XiaogeLiu ZiheKong LingyaoWang YihuanFang YudongGao LuLi YueZheng ZheLiu GangqiongFan Siyuan - To explore the role and mechanism of X-linked USP11 in mitochondrial dysfunction associated with depression. - Source: PubMed
Feng YuqiLi NingyuanZhang LingfengWang WeiDuan HaoSun SiqiLi RuilingZhang YuhuiSong XinhuaZhang YingyueZhang HonghanNie ZhaowenYan HanchunWang ChaoLiu Zhongchun - To explore the regulatory role of SENP1 in ferroptosis of differentiated thyroid cancer cells and its molecular mechanism. - Source: PubMed
Zhu FeifeiYan NaYang JiwenChen XiaoleiWang Yingying - Rta and Zta are transcription factors expressed by Epstein-Barr virus (EBV) during the immediate-early stage of the lytic cycle. While these two proteins do not interact directly, they bind to a scaffold protein, RanBPM, to synergistically activate the transcription of EBV lytic genes. Earlier studies have shown that both Rta and Zta are destabilized through ubiquitination, which plays a crucial role in influencing EBV's lytic development. It is also known that Rta's ubiquitination is facilitated by the ubiquitin E3 ligase, RNF4. In this study, we show that RNF4 also promotes the ubiquitination of Zta. Meanwhile, a deubiquitinase, ubiquitin-specific protease (USP11), is known to interact with RanBPM. When tethered to RanBPM, Rta and Zta are deubiquitinated and stabilized by USP11. While host cells may utilize ubiquitination as a defense mechanism to destabilize Rta and Zta, thereby restricting EBV proliferation, EBV exploits RanBPM and the deubiquitination of Rta and Zta as a counter-defense strategy that favors EBV lytic replication. This study uncovers the interplay between the host and the viral mechanisms involving RNF4 and USP11 in modulating EBV lytic progression.IMPORTANCEEpstein-Barr virus (EBV) is known to express two crucial transcription factors, Rta and Zta, which are essential for activating the transcription of viral lytic genes. These two proteins are indispensable for viral lytic proliferation. While Rta and Zta can function independently to promote transcription, they also cooperate synergistically, leading to robust expression of EBV lytic proteins. In an earlier study, we showed that this synergy requires the formation of a complex involving Rta, Zta, and RanBPM at the Zta response elements in EBV lytic promoters. Recent studies showed that, despite their importance, these transcription factors are destabilized by ubiquitination, potentially serving as a mechanism through which the host restricts EBV proliferation. This study shows that EBV exploits USP11, which interacts with RanBPM, to deubiquitinate and stabilize Rta and Zta. The stabilization by USP11 is critical for EBV to overcome host-imposed restrictions and maximize its lytic proliferation. - Source: PubMed
Publication date: 2026/05/21
Chen Chi-YuanChen Po-ChunLu Yi-ShanLin Xin-RuYang Ya-ChunLee Yi-KaiCheng Zi-YunChang Shu-YinChiu Ya-FangChang Li-Kwan