KIF3B antibody - C-terminal region (ARP33908_P050)
- Known as:
- KIF3B (anti-) - C-terminal region (ARP33908_P050)
- Catalog number:
- arp33908_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- KIF3B antibody - C-terminal region (ARP33908_P050)
Related genes to: KIF3B antibody - C-terminal region (ARP33908_P050)
- Gene:
- KIF3B NIH gene
- Name:
- kinesin family member 3B
- Previous symbol:
- -
- Synonyms:
- KIAA0359, FLA8, KLP-11
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1999-07-06
- Date modifiied:
- 2015-09-01
Related products to: KIF3B antibody - C-terminal region (ARP33908_P050)
Related articles to: KIF3B antibody - C-terminal region (ARP33908_P050)
- There is few research on which genes play an important role in tumors without lymph metastasis. This study aimed to identify candidate molecular alterations preferentially associated with N0-stage LUSC. - Source: PubMed
Publication date: 2026/08/31
Alipour MarzyehMoghanibashi MehdiNaeimi SirousMohamadynejad Parisa - MicroRNAs play wide roles in non-small cell lung cancer (NSCLC). To investigate the clinical value of miR-483-3p in NSCLC and its molecular target, 350 NSCLC patients were recruited in this study. RT-qPCR results showed that tumor histological expression of miR-483-3p progressively decreased as the tumor-node metastasis (TNM) stage increased. The receiver operating characteristic (ROC) curve displayed that histological miR-483-3p level can effectively distinguish NSCLC patients with high TNM stage (III) from those with low stage (I+II) (area under the ROC curve = 0.869). The Kaplan-Meier curve showed that NSCLC patients with low miR-483-3p expression demonstrated a lower 5-year overall survival rate. After adjusting for other confounding factors, multivariate Cox analysis further identified miR-483-3p as an independent protective factor for NSCLC survival. Mechanistically, RNA pull-down assay showed that upregulation of miR-483-3p was co-precipitated with KIF3B mRNA and inhibited its expression, thereby suppressing the malignant phenotypes of NSCLC cells and inducing apoptosis. In conclusion, downregulation of miR-483-3p serves as a poor prognostic marker in NSCLC, potentially affecting cancer progression by negatively regulating KIF3B. - Source: PubMed
Publication date: 2026/06/05
Yang JunfaWang Wenhua - Autoinhibition is a fundamental regulatory mechanism for kinesins, including the heterotrimeric kinesin-2 complex (KIF3A/KIF3B/KAP3), which mediates cytoplasmic cargo transport and anterograde intraflagellar transport. In mammals, kinesin-2 is essential for ciliogenesis and ciliary function. Although a structural model of autoinhibited kinesin-2 has been proposed, further validation and functional analysis are needed. Here, we elucidate the mechanism and functional importance of kinesin-2 autoinhibition using cell-based assays guided by structural predictions. Through knockout-rescue experiments with chimeric KIF3A-KIF3B subunits, we show that subunit-specific interactions between the motor domains and the C-terminal coiled-coil domains and adjacent tail β-hairpin motifs stabilize the autoinhibited state. Interestingly, these same C-terminal regions required for autoinhibition are required for stable heterodimerization of the motor. We further find that a flexible region within the coiled-coil stalk is required for this autoregulation and may facilitate the underlying conformation transitions. Furthermore, the capacity to autoinhibit directly correlates with the ability of mutant motors to support ciliogenesis, underscoring the significance of autoinhibition for motor function. Collectively, these findings define key subunit-specific interactions underlying kinesin-2 autoinhibition, identify elements that govern conformational transitions, and demonstrate that autoinhibition is essential for kinesin-2 function in ciliogenesis. - Source: PubMed
Publication date: 2026/05/21
Adams Jessica MSawe CalebEngelke Martin F - Intracellular transport is essential for neuronal organization, yet how motor proteins achieve cargo selectivity remains incompletely understood. Kinesin-2 motors transport diverse cargos through the heterotrimeric KIF3/KAP3 complex, but whether variations in assembly composition contribute to functional specificity has been unclear. This study provides evidence for heterogeneity in neuronal KIF3/KAP3 assemblies, including a KIF3B-enriched, KAP3-associated population in addition to the canonical KIF3A/B/KAP3 complex. Biochemical and cellular analyses support a preferential association between this KIF3B-enriched assembly and TRIM46, a protein required for axon initial segment organization. Structural analyses further suggest that differences in tail conformation accompany distinct assembly states and may underlie cargo selectivity. Together, these findings support a model in which compositional and structural diversity within kinesin-2 complexes contributes to spatially regulated transport during neuronal development. - Source: PubMed
Publication date: 2026/03/30
Jiang XuguangIchinose SotaroOgawa TadayukiYonezawa KentoShimizu NobutakaHirokawa Nobutaka - Rearranged during transfection (RET) kinase mutations are frequently observed in the context of human thyroid and lung cancer treatment. Moreover, a considerable amount of effort has been dedicated by the scientific community to the identification of highly potent and selective RET inhibitors. In this study, we identified a series of pyrazolo[1,5-a]pyridine derivatives, and compound 9 as a candidate drug that targets both wild-type (wt) RET and RET by structure-activity relationship (SAR) study. In addition, 9 exhibited remarkable antitumor activity at a dose of 10 mg/kg/day, indicating that it completely hindered the growth of tumors induced by BAF3-KIF3B-RET-WT xenografts. In summary, 9 can be demonstrated to act as a potential RET inhibitor, as well as a treatment for RET-related cancers. - Source: PubMed
Publication date: 2026/03/26
Pan LinHu YangxiaoTan FuxingFang QinghongChen JunyueZhang YingjunWu WanqingXie Hongming