Ask about this productRelated genes to: TPX2 antibody
- Gene:
- TPX2 NIH gene
- Name:
- TPX2 microtubule nucleation factor
- Previous symbol:
- C20orf2, C20orf1
- Synonyms:
- p100, DIL-2
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-29
- Date modifiied:
- 2019-01-21
Related products to: TPX2 antibody
Related articles to: TPX2 antibody
- Developing early-maturing maize varieties with improved tolerance to high-density planting is essential for enhancing yield in China. In this study, a unique panel of 498 cold-adapted early-maturing inbred lines were evaluated for ear length (EL) and ear diameter (ED) across two locations under contrasting planting densities in one growing season. Phenotypic analysis revealed abundant phenotypic variation in these ear traits among the tested lines, and there were significant correlations between environments. A total of 406,897 high-quality single nucleotide polymorphism markers (SNPs) were obtained from liquid chip analysis. Population structure analysis classified the early-maturing maize germplasm into 9 distinct genetic groups, with obvious genetic differentiation between groups. Linkage disequilibrium (LD) analysis demonstrated rapid LD decay and high genetic variation in the population. A genome-wide association study (GWAS) identified 380 quantitative trait loci (QTLs) for both ED and EL under two planting densities. In total, 138 and 89 annotated genes were identified within QTLs detected under normal and high-density planting conditions, respectively. Among them, (a TPX2 family protein) and (an OVATE family transcription factor), which were located close to the top SNPs for ED and EL under high planting density, were considered positional candidate genes based on their annotations. Furthermore, by integrating candidate gene analysis with selection signatures, we found that candidate genes detected under high-density planting conditions show signatures of ongoing selection during maize breeding. These findings identify candidate genes for future functional validation and breeding-oriented follow-up studies. - Source: PubMed
Publication date: 2026/09/16
Jiang LijingChen ShuaihengGao YuanZhang TieqiangWang HuiWang RenjieZheng AnboJiang MinxuWang YiZhang Hongwei - Microtubule organization during cell division requires coordinated regulation by microtubule-associated proteins and protein kinase signaling pathways. In animals, TPX2 (Targeting Protein for Xklp2) regulates spindle assembly by binding to and activating Aurora A kinase. In , individual TPX2-like (TPXL) proteins have been implicated in Aurora-associated functions, but whether the TPXL family members share common microtubule-associated properties and how TPXL-Aurora interactions differ across the family remain incompletely understood. Here, we investigated the structural and cellular relationships among the eight TPX2-like proteins (TPXL1-TPXL8), microtubules, and Aurora kinases. AlphaFold3-based structural prediction indicated that specific interaction sites between TPXL proteins and tubulins were revealed at the three-dimensional structure and atomic level, suggesting that all TPXL proteins contain a conserved TPX2 domain contributing to their predicted tubulin association. Transient expression analyses showed that TPXL1-TPXL8 localized to microtubule arrays during both interphase and cell division. Although microtubule-associated domain is predicted to be conserved across the family, individual TPXL members exhibit distinct localization patterns on spindles and phragmoplasts, suggesting potential functional specialization. Further structural prediction and experimental validation revealed that only TPXL2, TPXL3, TPXL4, and TPXL8 interacted with AUR1 (Aurora 1) and AUR2, whereas no detectable interactions were observed for the other TPXL members or for any TPXL protein with AUR3. Structural prediction of TPXL-AUR1-tubulin complexes were consistent with a possible arrangement in which TPXL proteins contact both AUR1 and tubulin. Together, our findings suggest that TPXL proteins have broad microtubule association and are coupled with selective Aurora kinase interaction to coordinate microtubule organization, providing a framework for future functional analysis of TPXL-Aurora-microtubule association during plant cell division. - Source: PubMed
Publication date: 2026/09/08
Cao ShilinChen YuyingWeng ZongkuanRen HaiyunDu Pingzhou - Bifunctional genomic loci can produce both coding and noncoding outputs, yet the proteins encoded by many such loci remain unexplored. Here, we identify MSEP, a previously uncharacterized ∼54-kDa protein translated from an open reading frame embedded within the antisense RNA locus ARHGEF17-AS1. MSEP localizes to the mitotic spindle and spindle poles, and disruption of its start codon increases spindle abnormalities. MSEP interacts with the spindle-assembly factor TPX2, and its depletion is accompanied by reduced TPX2 abundance. MSEP undergoes cell-cycle-dependent phosphorylation that is regulated by Aurora A and WEE1. Depletion of MSEP is also associated with diminished Aurora A abundance at spindle poles. Genetic uncoupling of MSEP translation from ARHGEF17-AS1 RNA expression supports largely distinct protein- and RNA-mediated pathways that converge on spindle-pole integrity. Together, these results support a bifunctional-locus model in which ARHGEF17-AS1 RNA and its encoded protein, MSEP, contribute to mitotic spindle integrity through distinct, parallel pathways. - Source: PubMed
Publication date: 2026/09/24
Mahale SagarChikne VaibhavAdithya NitinMohamed Mohamed ShamsudiinSetia MeenakshiSjövall DanielPrajapati BharatHallqvist AndreasKanduri MeenaKanduri Chandrasekhar - Animal cells assemble gigadalton-scale molecular complexes composed of ~200 proteins to build a functional centrosome during mitosis, ensuring faithful chromosome segregation. Although the molecular principles underlying centrosome assembly have been extensively studied, the minimal components required to reconstitute centrosome-like activity in living cells remain unknown. Here, we develop an optogenetic strategy that exploits Aurora A kinase clustering to assemble functional centrosome-like structures in human cells. Remarkably, these light-induced assemblies activate Aurora A, nucleate microtubules, and bypass the requirement for the canonical Aurora A scaffold Cep192. Mechanistically, we identify the evolutionarily conserved Aurora A partner TPX2 as an essential factor for Aurora A cluster-dependent microtubule nucleation. Furthermore, optogenetic Aurora A clustering significantly rescues spindle assembly defects associated with centrosome ablation. We term this approach Light-Induced Spindle Assembly (LISA). By directly coupling Aurora A activity to spatial clustering, LISA defines a minimal and tunable module capable of driving spindle assembly. More broadly, LISA provides a synthetic biology platform for dissecting the fundamental principles of Aurora A-dependent spindle assembly, a prominent feature of mitotic and meiotic spindle formation. - Source: PubMed
Publication date: 2026/09/15
Olakkal VigneshBalakrishnan MadhumithaKotak Sachin - Protein-protein interactions (PPIs) regulate essential cellular processes and represent an important class of therapeutic targets; however, discovering effective modulators of PPIs remains a formidable challenge. Although deep learning approaches have been widely explored for PPI modulator discovery, many rely on simplified representations that obscure interchain boundary information and fine-grained PPI-modulator interaction (PPIMI) patterns, limiting their robustness under distribution shifts. To address this challenge, we introduce TvTPPIMI, a framework that leverages learnable boundary tokens to encode partner-aware boundary information and models PPIMI at atom-residue resolution. In a case study targeting the AURKA-TPX2 interaction, TvTPPIMI prioritized putative modulatory candidates from a small-molecule screening library. Structure-based docking, attention analysis, multireplica molecular dynamics simulations, MM/GBSA binding free-energy estimation, and noncovalent interaction analyses provided post hoc physical support for the stable AURKA binding of selected candidates, highlighting CE02-6266 as the most favorable compound among the tested hits. Together, these results suggest that TvTPPIMI provides a generalizable computational framework with coarse-grained, attention-based interpretive cues for PPIMI prediction and can be integrated with structure- and dynamics-based analyses to support PPI modulator discovery. - Source: PubMed
Yang LanChen JingTan HongLiu FuruiFang ZhongchengYuan YajingWang HanSun HeqiLi JiayiWei DongQing