Ask about this productRelated genes to: NUMA1 antibody
- Gene:
- NUMA1 NIH gene
- Name:
- nuclear mitotic apparatus protein 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 11q13.4
- Locus Type:
- gene with protein product
- Date approved:
- 1993-03-05
- Date modifiied:
- 2015-08-17
Related products to: NUMA1 antibody
Related articles to: NUMA1 antibody
- This study aimed to identify novel mutations associated with the progression of gastric cancer by establishing patient-derived xenograft (PDX) models and performing comprehensive genomic characterization of these PDX models and their corresponding primary tumors. - Source: PubMed
Publication date: 2026/01/29
Kong LukeWang JieZheng JunqiYang XihuaSun RuifangKou JiahuiYao YujieLi FengWang FuhuaGuo Sutang - Mammalian oocyte maturation relies on the precise assembly of the acentrosomal spindle, and its disruption causes aneuploidy and developmental failure. Symplekin (SYMPK), a 3'-end processing scaffold with emerging functions in regulating chromosome dynamics, remains unexplored in oocytes. Here, we investigate whether SYMPK governs spindle dynamics and chromosome fidelity during meiotic maturation. We find SYMPK dynamically tracks spindle microtubules during oocyte maturation following germinal vesicle breakdown (GVBD). By generating oocyte-specific Sympk knockout mice, loss of SYMPK in oocytes yields complete female infertility and impaired oocyte quality. Sympk-deficient oocytes show a predominant metaphase I (MI) arrest, accompanied by disorganized spindle architecture and destabilized kinetochore-microtubule attachments. Furthermore, chromosome spreads indicate persistent spindle assembly checkpoint (SAC) activation, and pharmacologic SAC inhibition can partially restore meiotic progression but not spindle integrity in SYMPK-deficient oocytes. Mechanistically, immunoprecipitation-mass spectrometry in MI oocytes reveals that SYMPK interacts with the spindle regulators KIF20A and NUMA1, and is required for their proper localization to the spindle. Collectively, these findings establish that SYMPK supports KIF20A and NUMA1 to coordinate acentrosomal spindle organization, thereby safeguarding oocyte meiotic maturation and ensuring faithful female meiotic progression. - Source: PubMed
Publication date: 2026/01/09
Chen BeiZhou MofanWang JiaqiXiao JinxinChen YirongWang JinyingHe WenlinSong TianbaoLuo JinXie QingzhenLiu Cong - Lymph node (LN) metastasis is a strong predictor of tumor recurrence following pancreatectomy for localized pancreatic neuroendocrine tumors (PanNETs). However, most patients lack LN metastasis and many tumors recur. Tools to guide risk-adapted surveillance in this group are lacking. - Source: PubMed
Ventin MarcoArya ShahrzadZhang LitiGangi AlexandraFernandez Del-Castillo CarlosQadan MotazHendifar Andrew ECattaneo GiuliaLiguori LuigiOsipov ArsenSabbatino FrancescoNissen Nicholas NKosari KambizLillemoe Keith DWei Alice CHe JinZureikat Amer HFerrone Cristina R - Dynein is a minus-end-directed microtubule motor that transports a variety of cargoes. Cargo specificity is mediated by a class of adaptor proteins that bind to the interface between dynein and dynactin, along the length of the Arp1 filament of dynactin, and that co-activate the motor. NuMA, ninein, and ninein-like protein (Nlp) are cargo-adaptors that are involved in microtubule organization, rather than carrying portable cargoes. At the same time, ninein and Nlp are believed to be anchorage factors for gamma-tubulin ring complexes to the centrosome. Here, we discuss recent findings on the interaction of NuMA and ninein with the dynein/dynactin complex, and how these findings challenge earlier concepts on ninein-dependent microtubule organization via gamma-tubulin complexes. We do not intend to provide an encyclopedic review on NuMA and ninein, but rather develop a hypothesis about how conformational changes may regulate the activities and binding specificities of these two proteins. - Source: PubMed
Publication date: 2025/11/15
Guo KeyingMerdes Andreas - In the 40 years since the discovery of the CENP proteins, many studies have examined the role of these proteins and their interactions with other chromosomal proteins of the centromere and beyond. Together, these studies have yielded vast amounts of sequencing and proteomics data. Typically, each study has focused on a single question and the majority of each dataset remains largely unexplored. Often the interesting details of publicly deposited data are left behind, buried in archives online, while more and more new data are generated. Reanalysing these databases can represent a new paradigm for investigating diverse biological pathways in unprecedented detail. Here, we explore two publicly available pan-cancer proteomic datasets to compare proteins whose abundance correlates with CENP proteins, with a particular focus on CENP-C. Our analysis confirms an expected link between CENP-C and cohesin levels but reveals a surprising and unexpected correlation between CENP-C and proteins of the inner nuclear membrane and the NuMA protein. This guilt-by-association analysis has the potential to identify proteins that act in common pathways but never associate or colocalize and may not even be expressed at the same time in cells. As an example, we show here that it can reveal unexpected links that expand our conception of centromeric chromatin beyond chromosome segregation. - Source: PubMed
Publication date: 2025/11/25
Kochanova Natalia YSamejima ItaruEarnshaw William C