TUBB2B Over-expression Lysate
- Known as:
- TUBB2B Over-expression Lysate
- Catalog number:
- LY14150a
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- TUBB2B Over-expression Lysate
Related genes to: TUBB2B Over-expression Lysate
- Gene:
- TUBB2B NIH gene
- Name:
- tubulin beta 2B class IIb
- Previous symbol:
- -
- Synonyms:
- MGC8685, DKFZp566F223, bA506K6.1
- Chromosome:
- 6p25.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-11-03
- Date modifiied:
- 2015-12-17
Related products to: TUBB2B Over-expression Lysate
Related articles to: TUBB2B Over-expression Lysate
- Dandy-Walker malformation (DWM) is a condition characterized by a cyst in the posterior cranial fossa contiguous with the fourth ventricle, combined with complete or partial agenesis of the cerebellar vermis; and elevation of the cerebellar tentorium, torcular Herophili, and transverse sinuses. DWM has been linked to specific genetic variants, with pathogenic or likely pathogenic variants reported in FOXC1, ZIC1, and ZIC4. Variants in the TUBB2B and TUBB3 genes are associated with abnormalities in tubulin, leading to cerebellar hypoplasia. In our study, three patients diagnosed with DWM underwent whole-genome analysis using next-generation sequencing, and two were found to have heterozygous variants in the tubulinopathy-associated genes TUBB2B and TUBB3, respectively. These findings indicate that some cases previously diagnosed as DWM may fall under the spectrum of tubulinopathies associated with cerebellar hypoplasia. - Source: PubMed
Publication date: 2026/06/17
Ueno KatsuyaHigasa KoichiroHayashi MikioIsozaki HarunaMiyata MayukoNaito NobuakiLi YiTakeda JunichiNonaka Masahiro - To determine the diagnostic yield of comprehensive genetic testing in patients with neuroimaging findings suggestive of lissencephaly spectrum disorders and to characterize novel pathogenic variants contributing to the genetic architecture of the spectrum. - Source: PubMed
Meašić Ana-MariaVulin KatarinaBobinec AdrianaMorožin Pohovski LeonaSansović IvonaMikloš MoranaKero MijanaTripalo Batoš AnaOdak LjubicaBarišić Ingeborg - The Bone Morphogenetic Protein (BMP) family acts as a critical modulator of cellular plasticity and lineage commitment in oncogenesis. However, the systematic contribution of BMP-related mRNAs (BRMs) to the progression and immunophenotypic landscape of kidney renal clear cell carcinoma (KIRC) remains poorly defined. - Source: PubMed
Publication date: 2026/06/06
Zhou YajieHu ZijianXie LeiZhang ShuwenHuang QiZhang NanLiu YijiangZhang WenxiongWang Kang - The intracellular transport system is pivotal for cellular function and integrity, facilitated by cytoskeletal motor proteins such as dynein, which traverse along microtubules (MTs). The heterogeneity of the tubulin isotypes composing MTs introduces functional diversity, potentially affecting cytoskeletal motor proteins' interactions with the MT. This study investigated the influence of amino acid sequence variations in the C-terminal tails (CTTs) of six different tubulin isotypes, TUBB2A, TUBB2B, TUBB2C, TUBB3, TUBB4A, and TUBB5, highly expressed in human brain tumors, and assessed the isotypes' effect on the binding of motor protein dynein to MT. Among these isotypes, TUBB2A, TUBB2B, and TUBB2C were found to affect conformational motions of the dynein's microtubule-binding domain (MTBD) and stalk domain. The investigation highlighted the novel role of isotype-specific variations in lateral interactions between tubulin protofilaments (PFs) in determining the proximity of the β-CTT of the adjacent PF to the MTBD, potentially affecting dynein's motility and suggesting how changes in isotype expression directly influence dynein's velocity and processivity and contribute to transport defects associated with neurological disorders and cancers. Isolating specific tubulin isotypes experimentally is challenging due to their high sequence similarity and complex interactions with other microtubule-associated proteins. This makes it challenging to distinguish between different tubulin isotypes and their effects, particularly in tissues where multiple isotypes are coexpressed. Additionally, these isotypes are heavily modified by post-translational modifications, which further complicate the isolation of a single, unmodified tubulin isotype. As a result, computational approaches have been necessary in this study for exploring these effects in a controlled, isotype-specific manner. - Source: PubMed
Publication date: 2026/05/04
Garg JiveshLopes Ribeiro JuliaWallin StefanAlisaraie Laleh - Mammalian oocytes are filled with fibric structures called cytoplasmic lattice (CPL) that are essential for oocyte maturation and early embryonic development. CPL comprises subcortical maternal complex (SCMC) and multiple components, including PADI6. Although it was first discovered in the 1960s, the molecular architecture and assembly mechanisms of CPL remain poorly understood. Here we present the cryo-electron microscopy structure of CPL isolated from mouse oocytes. Our analysis identified 14 constitutive protein subunits and revealed that CPL is composed of repeating units comprising U-shaped basket (UB) and adapter ring (AR) features, forming a filamentous architecture. The AR adopts a two-fold symmetric conformation, containing two NLRP4F, four SCMC and two ZBED3 subunits circularized via two distinct interaction clusters. The UB is anchored by PADI6, a didecamer composed of ten homodimers assembled by two back-to-back pentamers, each forming the lateral side of the UB. The underfoot base and up and down sides of the UB are formed by multiple central-symmetric assemblies (UBE2D3-UHRF1-NLRP14) and (TUBB2B-TUBB2A-FBXW24-SKP1), respectively, associating with the PADI6 pentamers to construct the intact UB structure. Two SCMC dimers within each AR connect the up and down sides of two adjacent UBs with an extensive protein-protein interaction network, and thus maintain the repetitive connection between the neighbouring CPL units. Our work unveils the architectural principles underlying the assembly of this large, periodic CPL filament, offering a molecular basis for understanding the functions of CPL in early mammalian embryogenesis and female reproductive disorders. - Source: PubMed
Publication date: 2026/03/17
Liu ShuxianLiu YusongXue JunchaoLi ZhenzhenZhang YanLi BailunXu LidanLi LiliYu ZhenzhenYu HongtaoGao HaishanShen En-Zhi