Ask about this productRelated genes to: ZW10 antibody
- Gene:
- ZW10 NIH gene
- Name:
- zw10 kinetochore protein
- Previous symbol:
- -
- Synonyms:
- KNTC1AP
- Chromosome:
- 11q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-11
- Date modifiied:
- 2016-10-05
Related products to: ZW10 antibody
Related articles to: ZW10 antibody
- Immune dysfunction in the tumor microenvironment contributes to the progression of non-small cell lung cancer (NSCLC) in patients with chronic obstructive pulmonary disease (COPD). This study aimed to elucidate the roles of the RNA-binding protein Aly/REF export factor (ALYREF) and its target, ZW10 interacting protein (ZWINT), in mediating CD4 T cell dysfunction in this context. - Source: PubMed
Publication date: 2026/03/23
Li ShiMinSong QiDong FuShiLiu HaiYangMeng ShanShanHu Xin - Zeste White 10 (ZW10) is a key component of the spindle assembly checkpoint (SAC) that maintains chromosomal stability during mitosis. Dysregulation of ZW10 can cause chromosomal instability and aneuploidy-hallmarks of many cancers, including breast cancer, particularly triple-negative breast cancer (TNBC). However, its prognostic and therapeutic relevance in breast cancer remains unclear. - Source: PubMed
Publication date: 2026/03/11
Bellah Sm FaysalHossen Md AlimBillah Sm SakerDurojaye Olanrewaju AyodejiRaihan Md Obayed - Bladder cancer (BCa) is characterized by substantial molecular and clinical heterogeneity, hindering accurate prognostic assessment and treatment stratification. This study aimed to develop a machine learning-based prognostic model based on DNA repair-related genes and to investigate the functional relevance of representative genes in BCa. - Source: PubMed
Publication date: 2026/02/11
Liang ShijieLiu HaodongSu QishengLi XiaohongYang ZhengMo Wuning - Lipid droplets (LDs), originating from the ER, play critical roles in lipid metabolism. ER-LD contacts enable lipid exchange and support essential cellular processes. However, how viruses utilize ER-LD coordination remains elusive. Here, we demonstrate that hepatitis C virus (HCV) infection markedly increases LDs abundance and enhances ER-LD contacts. Through a targeted screen of ER-LD tethering proteins, we identified that the NRZ complex, composed of nonsteroidal anti-inflammatory drug-activated gene (NAG), RAD50 interactor 1 (RINT1) and zeste white 10 (ZW10), is essential for HCV-induced ER-LD association and viral infection. Mechanistically, RINT1 and ZW10 interact with the HCV envelope protein E1. Ectopic E1 expression is sufficient to promote ER-LD contacts, which are abolished upon NRZ depletion. NRZ depletion also impairs Dengue virus (DENV) and Zika virus (ZIKV) infection, suggesting its conserved proviral function. Together, this work uncovers a critical mechanism by which host inter-organelle tethering complexes regulate viral infection, offering new insights into virus-host interactions and potential antiviral targets. - Source: PubMed
Publication date: 2026/02/03
Li ZhifangXing YifanHuang XinyiTian BuyunMei JieFu XinyueHuang YuhanZhang QianDing BinbinCao XiaobaoXue YanhongLi ZonghongXu TaoJiu Yaming - We report that Aurora B kinase-mediated phosphorylation is essential for BubR1 acetylation at lysine 250 (K250), a modification required to preserve the mitotic checkpoint complex (MCC) and ensure accurate chromosome segregation. This Aurora B-BubR1 acetylation axis provides a mechanistic explanation for how kinetochore-microtubule attachment status is transduced to spindle assembly checkpoint (SAC) activity. Aurora B phosphorylates BubR1 at Serine 39 (and Ser16) in response to unattachment, and this phosphorylation is indispensable for subsequent K250 acetylation. Using a monoclonal anti-AcK250 antibody in structured illumination microscopy, we demonstrate that BubR1 acetylation sustains the fibrous corona, as shown by the crescent-shaped expansion of ZW10 and MAD2 surrounding kinetochores. Loss of either CENP-E or BubR1 acetylation abolishes fibrous corona, indicating that the interaction between acetylated BubR1 and CENP-E connects lateral attachment with the prevention of premature corona disassembly until proper end-on attachment is achieved. Disruption of Aurora B-mediated phosphorylation compromises K250 acetylation, fibrous corona maintenance, and MCC stability, whereas expression of a K250 acetylation-mimetic BubR1 rescues these defects in S16A/S39A phosphorylation-deficient mutants. Together, our findings establish a phosphorylation-acetylation cascade in BubR1 as a critical SAC signaling pathway and identify this axis as a promising therapeutic target in cancers driven by chromosomal instability. - Source: PubMed
Choi Si-YoungPark HaeminKim Sung-SooKim HyungminPark SanghyoLee Hyunsook