Ask about this productRelated genes to: RAB34 antibody
- Gene:
- RAB34 NIH gene
- Name:
- RAB34, member RAS oncogene family
- Previous symbol:
- -
- Synonyms:
- RAB39, RAH, NARR
- Chromosome:
- 17q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-09-14
- Date modifiied:
- 2017-04-21
Related products to: RAB34 antibody
Related articles to: RAB34 antibody
- Insulin secretion is a complex, vesicular transport process. Rab34 is a key regulator of intracellular vesicle transport; however, its role in insulin secretion has not yet been reported. miRNA-9 is vital for the development and progression of the diagnosis and treatment of type 2 diabetes. This study aimed to investigate whether miR-9 targets Rab34 to regulate insulin secretion in beta (β) cells and its molecular mechanism. We used miR-9 mimics, miR-9 inhibitors, and dual-luciferase reporter gene detection to prove that miR-9 is regulated by targeting Rab34 in Min6 cells. Transmission electron microscopy revealed a decrease in the number of insulin particles when Rab34 was overexpressed in β cells. Regarding the mechanism, Rab34 overexpression induced a decrease in the number of proinsulin-containing particles in β cells and significantly promoted proinsulin degradation. Immunofluorescence microscopy revealed that Rab34 overexpression resulted in insulin granule clustering. Conversely, Rab34 depletion maintained proinsulin and increased insulin secretion. miR-9 overexpression inhibited insulin secretion, and miR-9 downregulation promoted insulin secretion. Immunofluorescence results revealed that Rab34 induced insulin secretory vesicles toward the autophagic degradation pathway. Therefore, we concluded that miR-9 inhibits insulin secretion by promoting Rab34 expression, which regulates insulin secretion by mediating the degradation of proinsulin and autophagic degradation pathways in β cells. - Source: PubMed
Publication date: 2026/03/27
Guo Zhen-ZhenLi Ao-YingXiang Ting-TingZhang Zu-HaoDeng AoHan Yang - Ethylene oxide (E.O) is an ether compound that negatively affects male reproduction, specifically by impairing sperm function. However, the molecular mechanisms underlying the E.O-induced inhibition of sperm function remain poorly understood. Therefore, this study investigated the molecular mechanisms behind E.O-induced toxic effects on sperm motility by assessing Ras-associated binding (Rab) proteins. Therefore, 31 individual Duroc semen samples were analyzed to determine the correlations between Rab protein (Rab3A, Rab5, Rab14, Rab25, Rab27A, and Rab34) levels and sperm motility after exposure to 100-μM E.O. The results showed that E.O exposure significantly reduced sperm motility and motion kinematics. Furthermore, correlation analysis revealed that, in the control group, Rab3A, Rab5, Rab14, Rab25, Rab27A, and Rab34 levels were correlated with various sperm motion parameters. In contrast, only Rab3A and Rab14 levels correlated with multiple sperm motility and kinematic parameters in the 100-μM-E.O group. These results suggest that E.O may affect sperm motion parameters via the action of Rab proteins, leading to decreased sperm motility. Consequently, these findings provide important evidence of the molecular mechanisms underlying E.O-induced toxic effects on sperm function. - Source: PubMed
Publication date: 2026/01/12
Jo Jae-HwanClaudine UwamahoroJang Seung-IkJung Eun-JuLee Woo-JinBae Jeong-WonKim DaehyunMoon JoonhoNam Seung WonChung Eu JinYi JunkooKwon Woo-Sung - The primary cilium is a microtubule-based organelle that cycles through assembly and disassembly. In many cell types, formation of the cilium is initiated by recruitment of preciliary vesicles to the distal appendage of the mother centriole. However, the distal appendage mechanism that directly captures preciliary vesicles is yet to be identified. In an accompanying paper, we show that the distal appendage protein, CEP89, is important for the preciliary vesicle recruitment, but not for other steps of cilium formation (Kanie et al., 2025). The lack of a membrane-binding motif in CEP89 suggests that it may indirectly recruit preciliary vesicles via another binding partner. Here, we identify Neuronal Calcium Sensor-1 (NCS1) as a stoichiometric interactor of CEP89. NCS1 localizes to the position between CEP89 and the centriole-associated vesicle marker, RAB34, at the distal appendage. This localization was completely abolished in knockouts, suggesting that CEP89 recruits NCS1 to the distal appendage. Similar to knockouts, preciliary vesicle recruitment as well as subsequent cilium formation was perturbed in knockout cells. The ability of NCS1 to recruit the preciliary vesicle is dependent on its myristoylation motif and knockout cells expressing a myristoylation defective mutant failed to rescue the vesicle recruitment defect despite localizing properly to the centriole. In sum, our analysis reveals the first known mechanism for how the distal appendage recruits the preciliary vesicles. - Source: PubMed
Publication date: 2025/01/30
Kanie TomoharuNg RoyAbbott Keene LTanvir Niaj MohammadLorentzen EsbenPongs OlafJackson Peter K - Distal appendages are ninefold symmetric blade-like structures attached to the distal end of the mother centriole. These structures are critical for the formation of the primary cilium, by regulating at least four critical steps: preciliary vesicle recruitment, recruitment and initiation of intraflagellar transport (IFT), and removal of CP110. While specific proteins that localize to the distal appendages have been identified, how exactly each protein functions to achieve the multiple roles of the distal appendages is poorly understood. Here, we comprehensively analyze known and newly discovered distal appendage proteins (CEP83, SCLT1, CEP164, TTBK2, FBF1, CEP89, KIZ, ANKRD26, PIDD1, LRRC45, NCS1, CEP15) for their precise localization, order of recruitment, and their roles in each step of cilia formation. Using CRISPR-Cas9 knockouts, we show that the order of the recruitment of the distal appendage proteins is highly interconnected and a more complex hierarchy. Our analysis highlights two protein modules, CEP83-SCLT1 and CEP164-TTBK2, as critical for structural assembly of distal appendages. Functional assays revealed that CEP89 selectively functions in the RAB34 vesicle recruitment, while deletion of the integral components, CEP83-SCLT1-CEP164-TTBK2, severely compromised all four steps of cilium formation. Collectively, our analyses provide a more comprehensive view of the organization and the function of the distal appendage, paving the way for molecular understanding of ciliary assembly. - Source: PubMed
Publication date: 2025/01/30
Kanie TomoharuLiu BeibeiLove Julia FFisher Saxton DGustavsson Anna-KarinJackson Peter K - The precise role of lncRNAs in skeletal muscle development and atrophy remain elusive. We conducted a bioinformatic analysis of 26 GEO datasets from mouse studies, encompassing embryonic development, postnatal growth, regeneration, cell proliferation, and differentiation, using R and relevant packages (limma et al.). LncRNA-miRNA relationships were predicted using miRcode and lncBaseV2, with miRNA-mRNA pairs identified via miRcode, miRDB, and Targetscan7. Based on the ceRNA theory, we constructed and visualized the lncRNA-miRNA-mRNA regulatory network using ggalluvial among other R packages. GO, Reactome, KEGG, and GSEA explored interactions in muscle development and regeneration. We identified five candidate lncRNAs (Xist, Gas5, Pvt1, Airn, and Meg3) as potential mediators in these processes and microgravity-induced muscle wasting. Additionally, we created a detailed lncRNA-miRNA-mRNA regulatory network, including interactions such as lncRNA Xist/miR-126/IRS1, lncRNA Xist/miR-486-5p/GAB2, lncRNA Pvt1/miR-148/RAB34, and lncRNA Gas5/miR-455-5p/SOCS3. Significant signaling pathway changes (PI3K/Akt, MAPK, NF-κB, cell cycle, AMPK, Hippo, and cAMP) were observed during muscle development, regeneration, and atrophy. Despite bioinformatics challenges, our research underscores the significant roles of lncRNAs in muscle protein synthesis, degradation, cell proliferation, differentiation, function, and metabolism under both normal and microgravity conditions. This study offers new insights into the molecular mechanisms governing skeletal muscle development and regeneration. - Source: PubMed
Publication date: 2025/01/15
Wenlun WangChaohang YuYan HuangWenbin LiNanqing ZhouQianmin HuShengcai WuQing YuanShirui YuFeng ZhangLingyun Zhu