Ask about this productRelated genes to: RAB5A antibody
- Gene:
- RAB5A NIH gene
- Name:
- RAB5A, member RAS oncogene family
- Previous symbol:
- RAB5
- Synonyms:
- -
- Chromosome:
- 3p24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1990-01-22
- Date modifiied:
- 2015-06-29
Related products to: RAB5A antibody
Related articles to: RAB5A antibody
- Diabetic kidney disease (DKD) is a common condition with few treatment options, and inflammation plays a pivotal role in its progression. Luteolin, a natural compound found in traditional Chinese herbs, is known for its anti-inflammatory properties, making it a potential treatment for DKD. But its effect and mechanisms in DKD remain incompletely elucidated. - Source: PubMed
Publication date: 2026/04/24
Deng LingchenWang YongShi ChunruWu JieYao JinShen WanjunZhang ZiyueLiu RanWang XuZhu HanyuZhang LiCai GuangyanZhou JianhuiHong QuanChen Xiangmei - TBC (Tre2/Bub2/Cdc16) domain-containing proteins constitute the widespread family of GTPase-activating proteins (GAPs). They interact with the Rab superfamily of small GTPases, stimulate GTP hydrolysis, and regulate vesicle trafficking. TBC1D17, involved in Shiga toxin trafficking, autophagy and glucose metabolism regulation, constitutes an example of GAP interacting with Rabs. Here we present the first crystal structures of the murine and human TBC domains of TBC1D17 proteins determined at 2.20 and 3.34 Å resolution, respectively. The TBC domain in both structures represents a heart-like shape. Our analyses revealed dimerization of the TBC domain through a fragment located near residues participating in GTP hydrolysis, a result we observed also in structures of closely related homologs. Furthermore, we tested Rab5a interactions with various fragments of TBC1D17. Interestingly, this protein contains an annotated, yet uncharacterized, Rab-binding domain (RBD) and our studies revealed strong interactions of Rab5a with TBC1D17 fragments containing RBD, while interactions with the TBC domain alone are much weaker. These results provide the first direct evidence for the critical role of the TBC1D17 RBD in interactions with Rab5a. - Source: PubMed
Nielipińska DominikaOrlikowska MartaNielipiński MaciejSekuła BartoszBłażewska Katarzyna MGendaszewska-Darmach EdytaPietrzyk-Brzezińska Agnieszka J - Seed storage proteins (SSPs) are stored in protein storage vacuoles (PSVs) within plant endosperm cells. In rice, glutelins undergo post-Golgi trafficking via dense vesicles (DVs) to protein body II (PBII). Phosphatidylinositol 3-phosphate (PI3P) regulates endosomal, autophagic, and vacuolar trafficking, yet its role in glutelin transport remains unclear. Here, we characterized the glutelin precursor accumulation14 (gpa14) mutant, which exhibits over-accumulation of 57-kDa glutelin precursors and floury, shrunken endosperm. Map-based cloning identified a single adenine insertion in Vacuolar Protein Sorting 34 (OsVPS34), resulting in a putative truncated protein lacking the PI3Ka and PI3_PI4_kinase domains. OsVPS34 encodes phosphatidylinositol 3-kinase (PI3K), which interacts with other subunits of the PI3K complex to regulate the production of PI3P. PI3P was enriched in the trans-Golgi network (TGN) and pre-vacuolar compartment (PVC), co-localized with Rab5a and GPA5, and was detected in DVs and PBIIs. In gpa14, PI3P levels were reduced, leading to mis-localization and decreased membrane association of Rab5a and GPA5, key regulators of glutelin trafficking. Our findings demonstrate that OsVPS34 is essential for synthesis of PI3P, which plays a crucial role in recruiting GPA5 and Rab5a to DVs for glutelin post-Golgi trafficking in rice endosperm. - Source: PubMed
Publication date: 2026/03/18
Xu ShanbinMa MingqingZhao HuanhuanZhou AoniLi ZiLi BoHe YuzheZhang GuipingCai HongpingGu ChuanweiYu TingYang XueZhou LeiZhang YuDuan ErchaoTeng XuanLiu XiLiu ShijiaTian YunluJiang LingRen YulongWang YihuaDong HuiWan Jianmin - Endosomes are nanoscale intracellular compartments that sort and recycle cell-surface receptors such as epidermal growth factor receptor-1 (EGFR1). Nanometer-scale interactions and coclustering of signaling proteins, cargo, and the membrane are critical to this process, yet direct 3D visualization has been hindered by the limited resolution of conventional and super-resolution microscopies. Here, we adapt expansion microscopy (ExM) to visualize and quantify nanoclusters of endosomal proteins in human retinal pigment epithelial (RPE-1) cells. We developed a 3D distortion analysis leveraging the Farneback optical-flow principle to detect anisotropies in hydrogel expansion, revealing under-expansion of cytoplasmic regions within ExM hydrogels and overestimation of size and distance measurements of small compartments such as endosomes. To calibrate ExM images of cytoplasmic regions containing endosomes, we introduced a self-assembling protein nanocage that reports the true local nanoscale expansion factor. To stimulate and visualize EGFR1 internalization and sorting, we applied a pulse-chase protocol with fluorescently tagged epidermal growth factor (EGF), fixed cells at 15 and 30 min, and subjected samples to 10-fold ExM and multiplexed 3D Airyscan microscopy to map cargo and EGFR1 relative to other endosomal proteins. A volume tracing pipeline was developed to visualize the changes in the labeled EGF and EGFR1 densities at the limiting membrane of the endosomes. These changes included enrichment of EGF and EGFR1 in the endosomal interior and accumulation of Rab5a near the limiting membrane during early endosome maturation. Together, this multiplexed 3D ExM toolkit provides a quantitative framework for visualizing and measuring small subcellular organelles at true molecular-scale resolution. - Source: PubMed
Publication date: 2026/03/16
Shakespeare TaylaSeehra Rajpinder SFlores Rodriguez NeftaliAtuanya NkolikaSheard Thomas M DKöhler RalfBose DanielWunderley LydiaWoodman PhilipCiani BarbaraJayasinghe Izzy - Bovine Viral Diarrhea Virus (BVDV) poses a significant threat to the global cattle industry, causing substantial economic losses. Long non-coding RNAs (lncRNAs) play crucial regulatory roles in various biological processes, including viral infections. However, the specific lncRNAs influencing BVDV replication remain poorly characterized. This study identified lncSMIM14 as a key host factor upregulated during BVDV infection in MDBK cells. Functional analyses demonstrated that lncSMIM14 overexpression significantly enhanced BVDV replication, evidenced by increased viral mRNA levels, progeny virus titers, cytopathic effects, and dsRNA abundance, while its knockdown exerted the opposite effect. Mechanistically, we revealed that lncSMIM14 specifically targets and positively regulates the expression of the endocytosis-related GTPase Rab3a. Importantly, Rab3a itself was shown to be essential for efficient BVDV replication, as its overexpression promoted viral replication, and its knockdown inhibited it. Furthermore, Rab3a co-localized with key endocytic regulators Rab5a and Rab7a, and both lncSMIM14 overexpression and Rab3a overexpression promoted the formation of endocytic vesicles, particularly post-BVDV infection. Our findings unveil a novel mechanism wherein BVDV exploits the host lncRNA lncSMIM14 to hijack Rab3a-mediated endocytosis, facilitating its own replication. This study identifies the lncSMIM14-Rab3a axis as a critical host pathway subverted by BVDV, providing new potential targets for antiviral intervention. - Source: PubMed
Publication date: 2026/02/27
Shao ZhiranMa SiqiGao FengSiyueLou YangLiu XinyiYang LiMai ZhanhaiWang LixiaHaiyilati AreayiShi HuijunFu Qiang