Ask about this productRelated genes to: HAUSP antibody
- Gene:
- USP7 NIH gene
- Name:
- ubiquitin specific peptidase 7
- Previous symbol:
- HAUSP
- Synonyms:
- -
- Chromosome:
- 16p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-12
- Date modifiied:
- 2017-01-04
Related products to: HAUSP antibody
Related articles to: HAUSP antibody
- Transcriptional dysregulation in cancer is accompanied by an anabolic transcriptional response driving proliferation and metabolic adaptation. We previously found that oncogenic ETS variant transcription factor 4 (ETV4) overexpression is associated with DNA replication, glycolytic metabolism, tumor progression, and poor prognosis in non-small cell lung cancer (NSCLC). ETV4 is markedly overexpressed in multiple NSCLC datasets, including TCGA-LUAD and TCGA-LUSC. Importantly, ETV4 expression positively correlates with ubiquitin-specific protease 7 (USP7) and mitogen-activated protein kinase 7 (MAPK7) levels. While the E3 ligase constitutive photomorphogenesis protein 1 (COP1) is known to regulate ETV4 ubiquitination and degradation, ETV4 deubiquitination remains unclear. Our study reveals that USP7 deubiquitinates ETV4 and protects it from K11- and K48-linked ubiquitination and proteasomal degradation in NSCLC cells. ETV4 transcriptionally controls the expression of the MAPK pathway key gene MAPK7, which encodes extracellular signal-regulated kinase 5 (ERK5), and participates in the regulation of cell proliferation. Genetic knockdown or pharmacological inhibition of USP7 affects the transcriptional activity of ETV4 on its target gene MAPK7/ERK5. USP7 inhibitor P22077 significantly attenuates ETV4-MAPK7-induced cell proliferation in vitro and tumor growth in vivo. Furthermore, elevated ETV4, USP7, and ERK5 protein expressions are associated with poor prognosis of NSCLC patients. These findings identify that USP7 regulates the deubiquitination, stability, and transcriptional activity of ETV4, contributing to the malignant phenotype of ETV4. Inhibition of USP7 might be a promising target in NSCLC with the dysregulation of ETV4 or hyperactivated MAPK signaling. - Source: PubMed
Publication date: 2026/05/06
Meng XueZhang JiaxiZhang NingHou YuqiLi YimengKang JiaLi RuxinShi YinghuiWang JuanCheng LixinXing Lingxiao - The WASH complex regulates endosomal trafficking and is linked to several neurodevelopmental diseases, including Prader-Willi syndrome, Schaaf-Yang syndrome, and Hao-Fountain syndrome. Its function is tightly controlled by ubiquitination, maintained by the multi-subunit MUST complex containing both a ubiquitin ligase (MAGEL2/TRIM27) and a deubiquitinase (USP7). However, the mechanism underlying the MUST complex assembly remains poorly understood. In this study, we investigate the assembly of USP7 and MAGEL2 components of the MUST complex using NMR spectroscopy, isothermal titration calorimetry, X-ray crystallography, and cellular assays. We show that the USP7/MAGEL2 interaction is bipartite and multivalent. Two distinct domains of USP7, TRAF and UBL1-2, recognize two unstructured but evolutionarily conserved regions of MAGEL2, one of which contains multiple TRAF-binding sites. Furthermore, we determine the high-resolution crystal structure of the TRAF/MAGEL2 complex and identify Hao-Fountain syndrome-linked mutations in USP7 that disrupt USP7/MAGEL2 complex formation and in cells. These findings provide mechanistic insight into the pathogenic basis of Hao-Fountain syndrome and related Schaaf-Yang and Prader-Willi syndromes. - Source: PubMed
Publication date: 2026/04/28
Korchak Emilie JSoriano Gabriella ASemenova IrinaHao BingŠtepihar DenisBayat TaraFon Tacer KlementinaBezsonova Irina - Ubiquitin-specific protease 7 (USP7) is a deubiquitinating enzyme implicated in cancer development via stabilization of oncogenic proteins and immunosuppressive factors. We used a structure-based approach to design selective USP7 inhibitors to exploit this therapeutic target. Starting from allosteric USP7 ligand scaffolds, we introduced several structural modifications that generally preserved high inhibitory potency. Additionally, rigidification of a benzylic linkage mitigated off-target liability identified for the reference compound. This optimization led to the potent, USP7-selective lead compound (). Its pharmacokinetic profile in mice and preliminary safety assessments of the molecule encouraged us to use OAT-4828 as a tool compound for investigations. was well-tolerated in mice, demonstrating significant antileukemic activity in a syngeneic model of B-cell derived non-Hodgkin lymphoma. - Source: PubMed
Publication date: 2026/05/06
Chrzanowski JacekNowicka JulitaKoralewski RobertJoachimiak LukaszGzik AnnaBorek BartlomiejBrzezinska JoannaKusmirek DamianOlejniczak SylwiaMatyszewski KrzysztofMazur MarzenaOlczak JacekGlatt SebastianGrudnik PrzemysławWilk PiotrMuchowicz AngelikaKikulska AgnieszkaGluchowska Katarzyna MDrzewicka KatarzynaBelczyk-Ciesielska AgnieszkaWachowska MalgorzataSipak-Bujanowicz ZuzannaMulewski KrzysztofTkaczyk AgnieszkaRejczak TomaszGolebiowski AdamZaslona ZbigniewBlaszczyk Roman - CCAAT/enhancer-binding protein B (CEBPB) has been reported as a transcription factor implicated in the occurrence and development of various human tumors. However, its role and mechanism in hypopharyngeal squamous cell carcinoma (HpSCC) remain unclear. - Source: PubMed
Publication date: 2026/04/28
Li HonghuiFan RongQu YipingShao YuanBai YanxiaXu ChongwenHu JinsongZhang Xiaozhi - - Source: PubMed
Publication date: 2026/04/24
Pang WenguangFang MingxingWu Weidong