Ask about this productRelated genes to: Rab11B antibody
- Gene:
- RAB11B NIH gene
- Name:
- RAB11B, member RAS oncogene family
- Previous symbol:
- -
- Synonyms:
- H-YPT3
- Chromosome:
- 19p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-23
- Date modifiied:
- 2015-08-25
Related products to: Rab11B antibody
Related articles to: Rab11B antibody
- Influenza A virus (IAV) depends on host proteins to complete several important functions, including trafficking viral proteins throughout the cell. Previous work has established a critical role for the cellular vesicular trafficking protein, Rab11A, in transporting the viral genome segments to the site of budding at the plasma membrane. While the role of Rab11A in IAV assembly is relatively well understood, very little is known about the function of a closely related isoform (Rab11B) during influenza virus infection. We have shown that both Rab11A and Rab11B are required for successful IAV infection by current H1N1 or H3N2 isolates. Cells in which either Rab11A or Rab11B were depleted failed to efficiently produce virus, with significant reductions in infectious titer. Surprisingly, our data revealed that recent (2022) H3N2, but not H1N1, isolates failed to efficiently produce viral proteins in single-cycle infections when Rab11B (but not Rab11A) was depleted. Flow cytometry analysis suggests that the defect in protein production is driven by a reduction in the total number of infected cells, rather than a decrease in viral protein production at the single-cell level. Using reverse genetics and "7+1" reassortant viruses, we mapped this Rab11B-dependent early defect in recent H3N2 isolates to the HA gene. RT-qPCR analysis of H3N2 virions bound to the cell surface showed a ~50% decrease in virus binding to the surface of cells depleted of Rab11B, but not Rab11A. Analysis of cell surface α2,6 and α2,3 sialic acids revealed no significant global change in sialic acid profile upon the depletion of Rab11B. As H3N2 virions could be removed by exogenous neuraminidase, the totality of these data suggests that the H3N2 failure to bind is the result of a loss of one (or more) specific sialylated cell surface protein(s) upon Rab11B depletion, rather than a decrease in bulk α2,6 sialic acid levels. These data suggest a novel role for Rab11B during viral entry that is specific to H3N2 isolates.IMPORTANCEInfluenza A is a major human pathogen, which poses risks through both the continuous circulation of "seasonal" influenza viruses (H1N1 and H3N2 subtypes) as well as the emergence of novel pandemic strains from animal hosts. Here, we demonstrate that contemporaneous H3N2 (but not H1N1) subtypes enter human lung cells through a Rab11B-dependent mechanism. This is distinct from the well-known role of Rab11A later in the life cycle, where it mediates the transport of viral ribonucleoprotein complexes to the site of virion assembly. These findings are relevant for assessing the risk that recently emerged zoonotic influenza viruses can enter human lung cells. Our work suggests that H1N1 and H3N2 viruses enter via different routes, which are not dependent on sialic acid levels. Our data provide important foundational information for the growing number of Rab11-dependent viruses, as it suggests that the Rab11 isoforms can affect both viral entry and viral exit. - Source: PubMed
Publication date: 2026/06/02
Turner Allyson HJaffrani Sara AKubinski Hannah CAjayi Deborah POwens Matthew BFanuele Conor DMcTigue Madeline PAppenzeller Cailey LBowling AddingtonDespres Hannah WSchmidt Madaline MShirley David JCrothers Jessica WBarrantes-Reynolds RamiroBruce Emily A - Membrane trafficking through the trans-Golgi network has been shown to guide activation of the NLRP3 inflammasome. Rab11 GTPases and their effector Rab11-FIP2 regulate endosomal trafficking and retrograde transport. Here, we demonstrate that Rab11b and Rab11-FIP2 contribute to NLRP3 and pro-IL-1β stabilization during the inflammasome priming phase, which is followed by inflammasome activation. We show Rab11-FIP2 to promote TAK1 phosphorylation and TAK1-mediated activation of IKKβ, a process controlling NLRP3 translocation to the trans-Golgi network. Human NLRP3 and Rab11-FIP2 bind each other via their phosphatidylinositol-4 phosphate (PI4P)-binding domains KMKK and N-terminal C2 domain, respectively. We also provide evidence indicating that Rab11-FIP2 stabilizes NLRP3 on early endosomes, which is important for ASC speck formation. These findings provide insights into the mechanisms controlling stability and intracellular trafficking of NLRP3 in human macrophages. - Source: PubMed
Publication date: 2026/03/25
Gravastrand Caroline SYurchenko MariaKristensen StineSkjesol AstridChen CarmenUllmann SindreIqbal ZunairaDahlen Karoline RuudRasheed KashifNonstad UnniRyan LivEspevik TerjeHusebye Harald - Cervical cancer (CC) is one of the most prevalent gynecological malignancies. The expression and functional role of the long non-coding RNA () () in CC remain poorly understood. - Source: PubMed
Gu XueminYang YuanyuanZhang ZhixiaOuyang YiqinTong Xiaowen - Mild traumatic brain injury (mTBI) often produces persistent deficits, yet the molecular mechanisms driving chronic pathology remain undefined. - Source: PubMed
Publication date: 2026/01/26
Yadikar HamadAnsari Mubeen A - Endocytosis constitutes a fundamental cellular process governing development through coordinated regulation of plasma membrane remodeling and ciliogenesis, processes essential for cell shape changes and tissue development. Although Twist1 null embryos display complete cranial neural tube (NT) closure defects and conditional knockout in neuroectoderm disrupts cranial neural crest cell fate determination and delamination, the function of TWIST1 in NT morphogenesis remains unknown. We investigated the basis underlying neuroectodermal morphological abnormalities in TWIST1 mutant embryos, specifically the formation of ectopic lateral bending points and cellular disorganization, by examining Twist1's role in cilia formation, adherens junction integrity, and endocytic vesicle dynamics. - Source: PubMed
Publication date: 2026/01/06
Thomas DerrickHufft-Martinez Brittany MLalwani ZarnaPham ViElmeniawi MaryTran An JXu JianmingSaadi IrfanFakhouri Walid D