| 2000 |
RAB11B localizes to transferrin-positive recycling endosomes and is essential for recycling of internalized transferrin to the plasma membrane. Constitutively active (Q/L) and constitutively inactive (S/N) mutants both blocked transferrin recycling without affecting uptake; a prenylation-deficient mutant (ΔC) had no effect, indicating membrane association is required. |
GFP-tagged mutant overexpression, transferrin recycling assay, subcellular colocalization |
Experimental cell research |
Medium |
10942597
|
| 2003 |
RAB11B in PC12 cells colocalizes with secretory vesicle markers. GDP-bound RAB11B stimulates constitutive secretion and depletes vesicular stores, while GTP-bound RAB11B directly impairs Ca2+-triggered exocytosis, demonstrating a GTP-dependent switch between regulated and constitutive secretory pathways in neuronal/neuroendocrine cells. |
Transfected hGH reporter in PC12 cells, constitutively active/inactive RAB11B mutants, secretion assays |
The Journal of neuroscience |
Medium |
14627637
|
| 2003 |
Endogenous RAB11B localizes to an apical pericentrisomal compartment distinct from RAB11A in polarized epithelial cells (MDCK and gastric parietal cells); its distribution is less dependent on microtubules than RAB11A, and it does not substantially colocalize with transferrin or IgA cargo handled by RAB11A. |
Immunofluorescence of endogenous proteins, nocodazole/taxol perturbation, subcellular fractionation/coisolation |
Experimental cell research |
Medium |
14567990
|
| 2009 |
RAB11B (but not RAB11A) selectively regulates apical recycling of CFTR in polarized intestinal epithelial (T84) cells. GDP-locked RAB11B-S25N inhibited ~80% of cAMP-activated halide efflux and reduced apical membrane CFTR by 50%; constitutively active RAB11B-Q70L increased stimulated efflux; RNAi knockdown of RAB11B (not RAB11A) reduced anion conductance by 50%. |
Dominant-negative/constitutively active mutant expression, RNAi knockdown, halide efflux assay, cell surface biotinylation, biotin protection recycling assay, immunoisolation of vesicles |
Molecular biology of the cell |
High |
19244346
|
| 2011 |
RAB11B regulates apical recycling and surface expression of the epithelial sodium channel ENaC. Dominant-negative RAB11B (but not RAB11A) most effectively reduced basal and cAMP-stimulated ENaC-dependent Na+ transport; siRNA knockdown of RAB11B demonstrated its requirement for ENaC surface expression in mpkCCD cells. |
Dominant-negative mutant expression, siRNA knockdown, Ussing chamber Na+ transport assay, immunoisolation, confocal colocalization |
American journal of physiology. Renal physiology |
Medium |
22129970
|
| 2011 |
RAB11B (not RAB11A) limits plasma membrane density of Cav1.2 L-type Ca2+ channels by promoting their degradation. Dominant-negative RAB11B-S25N or shRNA knockdown of RAB11B increased peak L-type Ba2+ current by ~64–66% and increased surface Cav1.2 density; cell surface biotinylation showed the effect is on degradation, not anterograde trafficking. |
Dominant-negative mutant, shRNA knockdown, whole-cell patch clamp, cell surface biotinylation, HA-tagged channel |
American journal of physiology. Cell physiology |
Medium |
21248079
|
| 2011 |
RAB11B and its effector Rip11 regulate acidosis-induced trafficking of V-ATPase to the plasma membrane in salivary duct cells. RAB11B showed higher colocalization with V-ATPase than RAB11A; RAB11 (not RAB25) interacts with the ε subunit of V-ATPase; siRNA knockdown of RAB11B or Rip11 prevented acidosis-induced V-ATPase translocation. |
siRNA knockdown, confocal colocalization, co-immunoprecipitation (RAB11/V-ATPase ε subunit), immunofluorescence |
Journal of cellular physiology |
Medium |
20717956
|
| 2012 |
The cAMP/PKA/CREB signaling pathway controls acidosis-induced V-ATPase trafficking in salivary ducts via transcriptional regulation of RAB11B expression; PKA phosphorylates CREB which activates RAB11B transcription, and CREB loss-of-function downregulates RAB11B and impairs V-ATPase translocation. |
Pharmacological inhibitors/activators of PKA/Src/ERK, RT-PCR, immunoblotting, siRNA loss-of-function |
The international journal of biochemistry & cell biology |
Medium |
22561749
|
| 2013 |
RAB11B mediates keratinocyte-stimulated exocytosis of melanin (melanocores) from melanocytes, which is then endocytosed by keratinocytes. Depletion of RAB11B (but not RAB27A) markedly decreased both keratinocyte-stimulated melanin exocytosis and melanin transfer to keratinocytes. |
siRNA depletion of RAB11B vs RAB27A, electron microscopy of human skin, melanocyte-keratinocyte co-culture, functional transfer assay |
The Journal of investigative dermatology |
Medium |
24141907
|
| 2013 |
GRAB (RAB3IL1/Rabin3-like 1) is a direct binding partner of RAB11B (and RAB11A but not RAB25). The RAB11B-binding region of GRAB maps to its carboxy-terminus, distinct from its GEF domain. Exogenous expression of RAB11B shifts GRAB distribution from cytoplasm to membranes. A GRAB deletion mutant (GRABΔ223-228) is deficient in RAB11B binding. |
Co-immunoprecipitation, deletion mutagenesis, subcellular localization by microscopy |
Biochemical and biophysical research communications |
Medium |
24140058
|
| 2014 |
Crystal structure of the cGMP-dependent protein kinase II (PKG II) leucine zipper domain in complex with RAB11B was solved. The PKG II LZ domain dimerizes and interacts with RAB11B via a mostly nonpolar surface; contact surfaces in RAB11B include switch I and II, interswitch, and β1/N-terminal regions. This binding surface differs from the Rab11-family interacting protein (Rab11-FIP) complex surfaces. |
X-ray crystallography, mutagenic analysis, in vitro binding |
The Journal of biological chemistry |
High |
25070890
|
| 2015 |
RAB11B (not RAB11A) is required for recycling of PAR1 (protease-activated receptor-1). siRNA depletion of RAB11B blocks PAR1 recycling and enhances lysosomal degradation of the receptor; in RAB11B-depleted cells, enhanced PAR1 degradation is redirected through an autophagic pathway (blocked by co-depletion of RAB11A or ATG5). |
siRNA library screen (140 trafficking proteins), targeted siRNA knockdown of RAB11B vs RAB11A, receptor recycling/degradation assays, fluorescence microscopy |
The Journal of biological chemistry |
Medium |
26635365
|
| 2017 |
Two recurrent de novo missense mutations in RAB11B (p.Val22Met, p.Ala68Thr) alter the GTP/GDP binding pocket, produce localization patterns resembling inactive RAB11B, and induce RAB11B binding to the GEF SH3BP5, similar to inactive (GDP-bound) RAB11B, causing a neurodevelopmental syndrome with severe intellectual disability. |
3D protein structure modeling, subcellular localization studies, binary interaction assay with effectors/GEFs (including SH3BP5) |
American journal of human genetics |
Medium |
29106825
|
| 2020 |
RAB11B mediates recycling of integrin β1 to the cell surface, controlling the surface proteome during breast cancer brain metastatic adaptation. RAB11B-mediated integrin β1 surface expression enables engagement with brain ECM and activates mechanotransduction signaling for survival. Lipophilic statins prevent membrane association and activity of RAB11B. |
Time-course RNA-seq, Drosophila genetic screen, proteomic analysis of cell surface proteome, RAB11B loss-of-function, integrin β1 surface expression assays, statin treatment |
Nature communications |
Medium |
32541798
|
| 2020 |
RAB11B inhibits osteoclastogenesis by directing c-Fms and RANK surface receptors to lysosomes for proteolytic degradation via early endosome–late endosome–lysosome axis; RAB11B overexpression enlarges early and late endosomes and abolishes surface RANK/c-Fms, attenuating NFATc1 signaling. Lysosomal inhibitor chloroquine rescued receptor degradation. |
RAW-D and bone marrow macrophage differentiation assay, RAB11B overexpression, chloroquine inhibition, immunofluorescence, endosome size measurement |
International journal of molecular sciences |
Medium |
33302495
|
| 2021 |
RAB11B is an HSP90 client protein; RAB11B interacts with HSP90α and HSP90β in osteoclasts via the HSP90 ATPase domain (not requiring ATPase activity for turnover). Blocking HSP90–RAB11B interaction (by siHSP90 or 17-AAG) abrogates RAB11B-mediated lysosomal trafficking of c-Fms and RANK, thus alleviating RAB11B-dependent inhibition of osteoclastogenesis. |
Co-immunoprecipitation, siRNA knockdown, pharmacological inhibition (17-AAG), in vitro osteoclastogenesis |
Biochimica et biophysica acta. Molecular cell research |
Medium |
34242681
|
| 2021 |
RAB11B-AS1 lncRNA (acting as a natural SINEUP) increases endogenous RAB11B protein levels without affecting RAB11B mRNA, demonstrating post-transcriptional upregulation of RAB11B by its antisense transcript through translational enhancement. |
CHD8 knockdown neuronal model, RT-qPCR (mRNA levels), Western blot (protein levels), SINEUP functional assay |
Frontiers in genetics |
Low |
34880900
|
| 2023 |
RAB11A and RAB11B redundantly control mitotic spindle function in intestinal epithelial progenitor cells. Combined knockout of both (but not single knockouts) causes defective cell cycle entry, mitotic arrest, and apoptosis with complete lethality within 3 days. RAB11B immunoprecipitates contain mitotic spindle microtubule regulators including KIF11; RAB11 disruption impairs bipolar spindle formation. |
Conditional double-knockout mouse model, enteroid culture, proteomic immunoprecipitation, flow cytometry, electron microscopy of spindles |
EMBO reports |
High |
37424454
|
| 2025 |
RAB11B is required for mitochondrial structural and functional integrity in gut epithelial cells (specifically Paneth cells). Rab11b knockout mouse intestines show altered mitochondrial protein targeting, impaired mitochondrial membrane potential, increased ROS production, and severe mitochondrial membrane defects by electron microscopy; RAB11B-specific interactome contains mitochondrial regulators. |
Rab11b conditional knockout mouse, transcriptomics, proteomic interactome, flow cytometry (membrane potential/ROS), electron microscopy |
Frontiers in cell and developmental biology |
Medium |
40248353
|
| 2024 |
RAB11B promotes M1-like macrophage polarization in alcohol-associated liver disease by restraining autophagic degradation of NLRP3. RAB11B overexpression in macrophages inhibits autophagic flux, suppressing LC3B-mediated NLRP3 degradation; macrophage-specific RAB11B knockdown alleviates alcohol-induced liver inflammation. |
Macrophage-specific AAV knockdown, RAB11B overexpression in BMDM/RAW264.7, autophagic flux assay, immunofluorescence, in vivo ALD mouse model |
Acta pharmacologica Sinica |
Medium |
38992121
|
| 2025 |
RAB11B (but not RAB11A) is required for H3N2 influenza A virus binding and entry; depletion of RAB11B reduced H3N2 virion binding to the cell surface by ~50%. This phenotype maps to the HA gene of H3N2 via reverse genetics and is not due to global changes in sialic acid levels but likely reflects loss of a specific sialylated surface protein(s) normally maintained at the surface by RAB11B recycling. |
siRNA depletion, single-cycle infection, RT-qPCR of bound virions, flow cytometry, reverse genetics/reassortant viruses, neuraminidase treatment |
Journal of virology |
Medium |
42227759
|
| 2025 |
RAB11B (but not RAB11A) controls NLRP3 inflammasome activation in human macrophages downstream of RAB11-FIP2. RAB11-FIP2 interacts with NLRP3 via its N-terminal C2-domain (NLRP3 binds via KMKK motif); RAB11-FIP2 and RAB11B regulate caspase-1-mediated cleavage of pro-IL-1β and GSDMD and pyroptotic cell death on early endosomes; PI4P-positive endosome and ASC-speck formation are also controlled by this complex. |
Co-immunoprecipitation (FIP2-NLRP3 domain mapping), siRNA knockdown of RAB11B vs RAB11A, caspase-1 cleavage assay, GSDMD cleavage, pyroptosis assay, PI4P endosome imaging |
bioRxivpreprint |
Medium |
bio_10.1101_2025.05.19.654879
|