Ask about this productRelated genes to: PSMB2 antibody
- Gene:
- PSMB2 NIH gene
- Name:
- proteasome subunit beta 2
- Previous symbol:
- -
- Synonyms:
- HC7-I
- Chromosome:
- 1p34.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-03
- Date modifiied:
- 2016-10-05
Related products to: PSMB2 antibody
Related articles to: PSMB2 antibody
- Glioblastoma multiforme (GBM), a highly aggressive primary brain malignancy, is characterized by its accelerated development, refractoriness to therapy, and dismal prognosis. The proteasome subunit β2 (PSMB2), a catalytic unit of the 20S proteasome, has been linked to tumorigenesis across multiple malignancies; however, its signaling and therapeutic relevance in GBM remains incompletely defined. U87 and U251 GBM cells were engineered to overexpress (OE-PSMB2) or silence (Sh-PSMB2) PSMB2. We assessed the function of PSMB2 in GBM cell proliferation, migration, and related phenotypes, and further examined its association with the PTEN/PI3K/AKT signaling axis at both transcriptomic and protein levels. A xenograft model was conducted in the intracranial setting where the therapeutic efficacy of PSMB2 silencing, when used together with temozolomide (TMZ), was assessed. PSMB2 overexpression stimulated GBM cell proliferation, migration, and invasion, and PSMB2 silencing inhibited these phenotypes and promoted apoptosis. RNA-seq showed that PI3K/AKT pathway was enriched in Sh-PSMB2 cells. Protein-level analysis showed that PSMB2 expression was inversely associated with PTEN abundance and was accompanied by altered PI3K/AKT pathway activity. PSMB2 silencing decreased tumor burden and increased survival in vivo, and the combination of PSMB2 silencing and TMZ produced the greatest therapeutic effect. PSMB2 may function as a tumor-promoting regulator in GBM and is associated with PTEN/PI3K/AKT pathway modulation. Targeting PSMB2 suppressed tumor progression and enhanced the therapeutic response to TMZ in vivo, suggesting that PSMB2 may represent a potential therapeutic target for GBM. - Source: PubMed
Publication date: 2026/07/20
Tan ZiLongTang XiaolongChen ZhuoZhong YutingYe QinglinLi MinHe Wei - Sepsis is a life-threatening systemic inflammatory syndrome with limited targeted therapeutic options. Handelin, a natural compound derived from Chrysanthemum indicum, exhibits anti-inflammatory activity, yet its direct targets and protective mechanisms in sepsis remain unclear. - Source: PubMed
Publication date: 2026/03/19
Chen DexiuZhang QianWu YuanxinHu YingchunChen Muhu - Neddylation modifications in immune and tumor cells are linked to poor tumor prognosis. This study identifies prognostic genes associated with neddylation-related genes (NRGs) in colorectal cancer (CRC) using single-cell and spatial transcriptome (ST) sequencing, aiming to advance CRC treatment strategies. - Source: PubMed
Publication date: 2025/12/24
Zhu ZimingZhang XinyueWang SongHuang YunsiHan XuedongLai DongpingYao XinLan WeixuanNong HuiZeng WenbinMo YanhuaXu Ri'anZhang Tao - Nasopharyngeal carcinoma (NPC), highly prevalent in southern China, often leads to treatment failure in advanced stages due to recurrence or metastasis. While METTL14 plays a crucial role in cancer, its regulation of immune- and inflammation-related genes remains poorly understood. This study aims to investigate whether METTL14 is involved in regulating the expression of genes associated with tumor necrosis factor (TNF), interferon (IFN), interleukin (IL), and MHC class I in NPC cells. - Source: PubMed
Zhou ZhihaoWang JingShen LingjunHan LiuxinLi QiwenWu AibingLi JingLiang ZumingZhu LitongHe DanhuaZhou YingHuang ShihaoZhao ZhanlinCong JingePeng ZhitaoZhao PingYe ShunaBai BinyiHong XuanjiaDai GuanqiLei YeZhao WentaoJia JunshuangLin XiaolinXiao DongZhang YuqinLin Taoyan - Classical swine fever virus (CSFV), a highly virulent member of the genus, is one of the most significant pathogens within this group. Although uncoating is a prerequisite for productive infection, the molecular determinants orchestrating this process remain obscure. The Core protein, functioning as the viral nucleocapsid, plays a pivotal role in the uncoating cascade. This study delineates a SUMOylation-dependent, ubiquitin-independent proteolytic mechanism essential for CSFV uncoating. The valosin-containing protein (VCP/p97) preferentially associates with SUMO1-modified Core, directing it toward degradation via the 26S proteasome, specifically through engagement with PSMB2 and PSMD2 subunits. Site-directed mutagenesis of the SUMOylation motif abolishes VCP-mediated degradation, substantiating its functional indispensability. Fluorescent tracking of CSFV virions using molecular beacon and quantum dot labeling further reveals that VCP governs the endosomal trafficking of viral particles from early to late endosomes-an essential step for capsid disassembly and genome release. Moreover, VCP operates in concert with NPL4 and UFD1, enabling the translocation of SUMOylated Core toward the proteasomal machinery. Collectively, these findings uncover a previously uncharacterized SUMO1-VCP-PSMB2/PSMD2 axis that couples intracellular trafficking with proteasomal disassembly of the CSFV Core, providing mechanistic insights into uncoating and nominating host factors as promising antiviral targets. - Source: PubMed
Publication date: 2025/11/25
Zou Lin-KeBai Ji-ShanSun Rui-CongYang Han-FeiWan Ming-YueZhao Bing-QianSun Bo-TaoChen Jin-XiaChen JingCheng YanZhou Bin