Anti - Mouse, Cyclin D1 Clone AM29
- Known as:
- Anti - Mouse, Cyclin D1 Clone AM29
- Catalog number:
- 61-0021
- Product Quantity:
- 1 mL
- Category:
- -
- Supplier:
- Genemed
- Gene target:
- Anti - Mouse Cyclin D1 Clone AM29
Related genes to: Anti - Mouse, Cyclin D1 Clone AM29
- Gene:
- HAUS6 NIH gene
- Name:
- HAUS augmin like complex subunit 6
- Previous symbol:
- FAM29A
- Synonyms:
- FLJ20060, KIAA1574, dgt6
- Chromosome:
- 9p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-06
- Date modifiied:
- 2015-11-09
Related products to: Anti - Mouse, Cyclin D1 Clone AM29
Related articles to: Anti - Mouse, Cyclin D1 Clone AM29
- The HAUS augmin like complex subunit 6 (HAUS6) is associated with cytokinesis.HAUS6 has only been reported in a few cancers. To date, there are no published studies about the potential biological features and clinical meaning of HAUS6 in pan-cancer. - Source: PubMed
Publication date: 2025/11/24
Xie HaixiangWan ZuyinLu XianweiYang KejianQin ChongjiuChen YuLan ChenluPeng KaiQin WeiMo ShutianZhou XinYang ChengkunLiao XiwenPeng Tao - How microtubules (MTs) are generated in the proper orientation is essential to understanding how the cytoskeleton organizes a cell and MT-dependent events such as cell division. In the spindle, most MTs are generated through the branching MT nucleation pathway. In this pathway, new MTs are nucleated from the side of existing MTs and oriented at a shallow angle by the branching factor augmin, ensuring that both MTs have the same polarity. Yet, how augmin binds MTs and sets the branch angle has remained unclear. Here, we report the cryo-electron microscopy structure of an augmin subcomplex on the MT. This structure resembles that of NDC80 bound to the MT, with the conserved CH domain of augmin's Haus6 subunit directly proximal to the MT lattice. We find that the Haus6 CH domain is a bona fide MT binding site that increases augmin's affinity for the MT and helps establish branch angle. A second binding site, located in the disordered N-terminus of Haus8, also establishes branch angle,. Thus, we find that augmin regulates MT branching using two domains, each tuned to modulate MT affinity and MT branch angle. This work expands our mechanistic understanding of branching MT nucleation and thus spindle formation. - Source: PubMed
Publication date: 2025/10/31
Travis Sophie MKraus JodiMcManus Collin TGolden KianaZhang RuiPetry Sabine - Branching microtubule nucleation is a key mechanism for mitotic and meiotic spindle assembly and requires the hetero-octameric augmin complex. Augmin recruits the major microtubule nucleator, the γ-tubulin ring complex, to pre-existing microtubules to direct the formation of new microtubules in a defined orientation. Although recent structural work has provided key insights into the structural organization of augmin, molecular details of its interaction with microtubules remain elusive. Here, we identify the minimal conserved microtubule-binding unit of augmin across species and demonstrate that stable microtubule anchoring is predominantly mediated via the calponin homology (CH) domain in Dgt6/HAUS6. Comparative sequence and functional analyses in vitro and in vivo reveal a highly conserved functional role of the HAUS6 CH domain in microtubule binding. Using cryo-electron microscopy and molecular dynamics simulations in combination with AlphaFold structure predictions, we show that the D. melanogaster Dgt6/HAUS6 CH domain binds microtubules at the inter-protofilament groove between two adjacent β-tubulin subunits and thereby orients augmin on microtubules. Altogether, our findings reveal how augmin binds microtubules to pre-determine the branching angle during microtubule nucleation and facilitate the rapid assembly of complex microtubule networks. - Source: PubMed
Publication date: 2025/08/22
Würtz MartinTonon GiuliaVermeulen Bram J AZezlina MajaGao QiNeuner AnnettSeidl AngelikaKönig MelanieHarkenthal MaximilianEustermann SebastianErhardt SylviaLolicato FabioSchiebel ElmarPfeffer Stefan - Spindle bipolarization, the process of a microtubule mass transforming into a bipolar spindle, is a prerequisite for accurate chromosome segregation. In contrast to mitotic cells, the process and mechanism of spindle bipolarization in human oocytes remains unclear. Using high-resolution imaging in more than 1800 human oocytes, we revealed a typical state of multipolar intermediates that form during spindle bipolarization and elucidated the mechanism underlying this process. We found that the minor poles formed in multiple kinetochore clusters contribute to the generation of multipolar intermediates. We further determined the essential roles of HAUS6, KIF11, and KIF18A in spindle bipolarization and identified mutations in these genes in infertile patients characterized by oocyte or embryo defects. These results provide insights into the physiological and pathological mechanisms of spindle bipolarization in human oocytes. - Source: PubMed
Publication date: 2024/08/23
Wu TianyuLuo YuxiZhang MeilingChen BiaobangDu XingzhuGu HaoXie SiyuanPan ZhiqiYu RanHai RuiqiNiu XiangliHao GuiminJin LipingShi JuanziSun XiaoxiKuang YanpingLi WenSang QingWang Lei - To explore the expression of HAUS6 in squamous cell carcinoma of the tongue (TSCC) and its relationship with the clinicopathological features of patients, and to further provide new ideas and therapeutic targets for curing TSCC. - Source: PubMed
Publication date: 2024/05/12
Yao ZhuoyueChen JingWang YueCao Liyu