Ask about this productRelated genes to: RAB8B antibody
- 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 antibody
Related articles to: RAB8B antibody
- 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 - Optineurin (OPTN) is a multifunctional adaptor protein involved in vesicular trafficking and selective autophagy. In this study, we investigated the molecular mechanism by which OPTN regulates these distinct processes through the leucine zipper (LZ) domain. OPTN interacts with the active form of RAB8A and closely related RAB proteins (RAB8B and RAB10). We determined the crystal structure of the OPTN-RAB8A complex at 1.83 Å resolution and elucidated the specific interaction mechanism between these proteins. Structure-guided mutational analysis at the molecular and cellular level suggested that OPTN interacts with RAB8A on two distinct surfaces. RAB8A-interacting surfaces of OPTN include residues that are located apart from the LZ-forming region. Furthermore, the interaction between OPTN and RAB8A was corroborated by cell biological approaches. Although RAB8A/8B/10 were not essential for mitophagy in experiments using their triple knockout cells, the RAB8A-binding residues of OPTN were critical for the recruitment of ATG9A vesicles. Therefore, our results provide molecular insights into the functional role of the LZ domain of OPTN in regulating vesicular trafficking and selective autophagy. - Source: PubMed
Okatsu KeiKikuchi ReikaMatsuda NoriyukiFukai ShuyaYamano Koji - : Previous proteomic studies provided valuable information about cataracts, but unclarified issues, such as sex and ethnicity-associated differences, remain. This study aimed to provide additional data on cataract-related proteins regarding age, sex, and cataract type. : Twenty-six female and seven male Turkish cataract patients were screened for visual acuity and dysfunctional lens index. A nano-LC-MS/MS system and Progenesis QI software v3.0 were used for protein identification and quantification. The remaining data were evaluated with SPSS Version 29.0 software. : Proteins that showed age-associated changes were mainly involved in cytoskeletal organization. A glyoxalase enzyme, caveolin 1, and HS90B were lower, and RAB8B and ATP6V1B1 were higher in lenses in women. Proteins with lower levels in cataractous lenses than in transparent lenses included filensin and phakinin, concurrent with previous publications, and LCTL, GDI, HSPB1, and EIF4A2, not reported before. Corticonuclear cataracts constituted the only group showing depletions in putatively protective proteins, while the cortical type was the least influenced. ANXA1 and DNHD1 positively, and TCPD, SEC14L2, and PRPS1 proteins negatively correlated with visual acuity. : This study revealed cataract-related proteins concurrent with earlier studies and new ones hitherto unreported. Despite the low number of patients investigated, the results merit further research, as these new proteins are highly likely to be involved in cataractogenesis. - Source: PubMed
Publication date: 2025/07/04
Cosar BanuNefesoglu Mustafa SehvarAltinoz Meric AAkgun EmelSahin BetulBaykal AhmetSerteser Mustafa - Over 2.6 million adults over the age of 65 develop delirium each year in the United States (US). Delirium is associated with a significant increase in mortality and the US health care costs associated with delirium are estimated at over $164 billion annually. Despite the prevalence of the condition, the molecular pathophysiology of delirium remains unexplained, limiting the development of pharmacotherapies. Delirious patients can be identified by prominent impairments in attention and working memory (WM), two cognitive domains that localize to the dorsolateral prefrontal cortex (dlPFC). The dlPFC is also a key site for Alzheimer's disease (AD) pathology, and given the high risk of delirium in AD patients, suggests that efforts at understanding delirium might focus on the dlPFC as a final common endpoint for cognitive changes. Preclinical studies of the dlPFC reproduce many of the pharmacological observations made of delirious patients, including sensitivity to anticholinergics and an 'inverted U' pattern of dependence on monoaminergic input, with diminished performance outside a narrow range of signaling. Medications like guanfacine, which influence the dlPFC in the context of attention-deficit/hyperactivity disorder (ADHD), have emerged as therapies for delirium and motivate a detailed understanding of the influence of α-2 agonists on WM. In this review, I will discuss the neural circuitry and molecular mechanisms underlying WM and the function of the dlPFC. Localizing the cognitive deficits that are commonly seen in delirious patients may help identify new molecular targets for this highly prevalent disease. - Source: PubMed
Publication date: 2023/11/10
Lyman Kyle A