Ask about this productRelated genes to: RAB8B Blocking Peptide
- Gene:
- RAB8B NIH gene
- Name:
- RAB8B, member RAS oncogene family
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 15q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-29
- Date modifiied:
- 2016-10-05
Related products to: RAB8B Blocking Peptide
Related articles to: RAB8B Blocking Peptide
- The central nervous system responds to acute injury with plastic remodeling of its network. However, the temporal and structural dynamics of this response in the denervated dentate gyrus remain poorly understood. Therefore, we examined the transcriptional programs activated after perforant path transection, focusing on the outer molecular layer (OML) and the granule cell layer (GCL). - Source: PubMed
Publication date: 2026/05/19
Schlaudraff JessicaDel Turco DomenicoKey JanaDeller ThomasAuburger Georg - Immunogenic cell death (ICD) is an important regulatory form of cell death, which can trigger anti-tumor immune responses and plays a crucial role in the development of cancer. Gastric cancer (GC) is a highly malignant tumor with poor prognosis. Currently, there is still a need to explore effective prognostic markers for clinical risk stratification. Therefore, this study aims to identify key prognostic genes related to ICD and construct a novel prognostic signature for the prognosis assessment of GC. - Source: PubMed
Publication date: 2026/02/26
Wan QianZhang LingZheng XiaQian Jun - Lung adenocarcinoma (LUAD), the most widely existing subtype of non-small cell lung cancer (NSCLC), is a leading cause of cancer-related mortality, characterized by challenging early diagnosis, high rates of recurrence and metastasis, and poor prognosis. Chemotherapy remains the primary treatment for advanced LUAD, but its effectiveness is often hindered by the development of chemoresistance. In this study, a targeted metabolomics method unveiled a marked up-regulation of glycolysis in chemotherapy-resistant LUAD cells. Particularly, the ratio of fructose 1,6-bisphosphate (FBP) to fructose 6-phosphate (F6P) reflected the activity of the rate-limiting enzyme phosphofructokinase muscle isoform (PFKM) was significantly elevated. We further observed a significant increase in exosome release in chemotherapy-resistant cells. More importantly, it was found that the interaction between PFKM and exosomes plays a role in regulating chemoresistance in LUAD. Mechanistically, PFKM influences exosomes release by modulating Ras-related protein Rab-8B (RAB8B) expression, impacting apoptosis and glycolytic metabolism, thereby promoting chemoresistance. Furthermore, drug-resistant cells enhance chemoresistance in sensitive cells by releasing exosomes with heightened glycolytic activity. These findings highlight the crucial role of the PFKM-RAB8B axis in promoting chemoresistance, suggesting it as a potential therapeutic target for countering LUAD chemoresistance. - Source: PubMed
Publication date: 2025/09/12
Wang QiangNong QiyaoZang JunguoGao MeiyuZhang YingHao XinyuanTian YuanXu FengguoZhang Pei - Severe COVID-19 involves hyperinflammation and multiorgan pathology, but consistent gene signatures remain elusive. We aimed to identify consensus transcriptomic signatures and molecular mechanisms in severe COVID-19. We performed an integrative analysis of 39 studies spanning 11 tissue types, 1551 bulk RNA-seq samples, and over 2 million single cells. A vote-counting strategy combined with a systems-biology approach was applied to detect consensus differentially expressed genes (DEGs). Pathways related to interferon/TNF-α signaling, hypoxia response, and platelet activation were consistently enriched across data sets. Among consensus DEGs-such as IFITM3, BCL2A1, CAMK2D, and CCR1-RAB8B was prioritized for functional validation based on its recurrence in ~45% of tissues and its known role in vesicle trafficking, a process intimately linked to viral life cycles. Molecular dynamics simulations and in vitro assays in SARS-CoV-2-infected CaCo-2 cells demonstrated that RAB8B modulates VAMP-3 clustering and intracellular trafficking. Silencing of Rab8b-1 and Rab8b-2 reduced viral infection by 30% (p = 0.0302) and 76% (p < 0.001), respectively. This study defines robust consensus signatures and positions RAB8B as a critical host factor and potential therapeutic target in severe COVID-19. Further exploration of RAB8B inhibitors is warranted to explore therapeutic utility. An interactive database at https://covidatlas.sysbio.tools/. - Source: PubMed
Avila Jonathan PeñaPark PeterSingh YouvikaAmaral Paulo PCastro ÍcaroTen-Caten FelipeSchuch VivianeGonçalves André N AGiddaluru JeevanMorais Mauro César CafundóOgava Rodrigo L TLubiana Thiagode Castro Gabriel AmorosoAquino RodrigoDurão LuizMartins Júlia RaspanteJimenez LeandroCosta-Martins André GGonzalez-Dias PatríciaHirata Thiago Dominguez CrespoDias Thomaz LüscherPeixe Débora GuerraSimizo AdrianaE Silva Juan Carlo SantosVasconcelos Amanda PereiraRodrigues Marcelo BerçotCastelucci Bianca GVirgillio-da-Silva João VictorMenezes LarissaMoraes-Vieira Pedro MCabral-Marques OtavioNakaya Helder I - DENN/MADD (mitogen-activated protein kinase-activating death domain), a differentially expressed in normal and neoplastic cells (DENN) domain-containing protein functions in membrane trafficking. DENN domain-bearing proteins have guanine nucleotide exchange factor activity toward Rab GTPases. Here, we identify Rab GTPase substrates for DENN/MADD using a cell-based assay involving DENN domain-mediated recruitment of Rab substrates to mitochondria. We confirmed known interactions of DENN/MADD with Rab3A, Rab3B, Rab3C, Rab3D, and Rab27B and identified four new potential substrates, Rab8B, Rab15, Rab26, and Rab37, results confirmed with biochemical experiments. Mutations in the DENN domain of DENN/MADD result in diverse pathophysiological manifestations, ranging from predominant neurological dysfunction to a multisystem disorder. Structural analysis using AlphaFold suggested that these mutations affect DENN/MADD's interaction with Rab GTPases. Introducing such mutations into DENN/MADD's DENN domain influenced the mitochondrial recruitment of Rabs. This study identifies new DENN/MADD protein interactions and cellular pathways, the disruption of which results in human disorders. - Source: PubMed
Publication date: 2025/08/12
Khan MaleehaKumar RahulTrempe Jean-FrançoisFrancis VincentBanks EmilyAyoubi RihamLuna Luis AguileraMcPherson Peter S