| 1999 |
RAB11A localizes to an apical pericentriolar endosomal compartment in MDCK epithelial cells that is dependent on intact microtubules for its integrity; this compartment is accessible to membrane-bound markers internalized from either apical or basolateral poles, functionally defining it as the apical recycling endosome. |
Immunofluorescence, nocodazole treatment, dimeric IgA trafficking assay |
Molecular biology of the cell |
High |
9880326
|
| 2000 |
A dominant-negative GTP-binding-deficient RAB11A mutant (Rab11aS25N) potently inhibits both transcytosis and apical recycling of IgA but not basolateral transferrin recycling in polarized MDCK cells; conversely, GTPase-deficient RAB11A (S20V) inhibits basolateral-to-apical transcytosis but not recycling. This defines RAB11A's GTPase cycle as essential specifically for apical recycling and transcytotic pathways. |
Inducible expression of dominant-negative and constitutively active RAB11A mutants, IgA transcytosis assay, transferrin recycling assay |
The Journal of biological chemistry |
High |
10869360
|
| 1999 |
RAB11A is associated with H+/K+-ATPase-enriched gastric microsomes at a stoichiometry of approximately one RAB11A per six H+/K+-ATPase copies; expression of dominant-negative RAB11A N124I in primary parietal cells inhibits histamine-stimulated recruitment of H+/K+-ATPase to the apical membrane. |
Mass spectrometry co-fractionation, adenoviral dominant-negative expression, aminopyrine uptake assay, immunocytochemistry |
The American journal of physiology |
High |
10484323
|
| 1998 |
RAB11A redistributes to the apical secretory canaliculus during histamine stimulation of gastric parietal cells but does not dissociate into soluble fractions during vesicle fusion, indicating it remains membrane-associated through the tubulovesicle–canaliculus fusion cycle. |
Subcellular fractionation, immunofluorescence of resting vs. stimulated parietal cells |
The American journal of physiology |
Medium |
9688847
|
| 2002 |
After agonist-induced internalization, the M4 muscarinic acetylcholine receptor (M4 mAChR) traffics to transferrin receptor- and RAB11A-positive perinuclear recycling endosomes; dominant-negative RAB11A (S25N) inhibits M4 recycling to the cell surface, and expression of the myosin Vb C-terminal tail (a RAB11A effector) enhances M4 accumulation in perinuclear endosomes and impairs recycling. |
Fluorescence co-localization, dominant-negative RAB11A expression, myosin Vb tail overexpression, receptor recycling assay |
The Journal of neuroscience |
Medium |
12427833
|
| 2005 |
RAB11A and myosin Vb are required for bile canalicular formation in polarized hepatic WIF-B9 cells; knockdown of RAB11A or expression of GDP-locked RAB11A prevents canalicular formation, as does overexpression of the myosin Vb motorless tail domain. |
siRNA knockdown, dominant-negative overexpression, confocal imaging, polarized hepatic cell model |
Proceedings of the National Academy of Sciences of the United States of America |
High |
16214890
|
| 2006 |
RAB11A directly interacts with TRPV5 and TRPV6 Ca2+ channels in the GDP-bound conformation, co-localizing in vesicular structures beneath the apical plasma membrane; co-expression of GDP-locked RAB11A reduces cell surface expression and Ca2+ uptake of these channels. |
Co-immunoprecipitation, yeast-two-hybrid, Ca2+ uptake assay, dominant-negative RAB11A co-expression |
Molecular and cellular biology |
Medium |
16354700
|
| 2007 |
RAB11A co-localizes with CFTR in apical recycling endosomes in polarized human airway epithelial cells; endogenous CFTR forms a complex with endogenous myosin Vb and RAB11A; myosin Vb silencing or expression of a dominant myosin Vb tail fragment (which requires RAB11A interaction to exert its effect) decreases CFTR apical membrane expression and reduces Cl− secretion. |
Co-immunoprecipitation of endogenous proteins, siRNA knockdown of myosin Vb, dominant-negative myosin Vb tail fragment expression, electrophysiology (Cl− secretion assay), surface biotinylation |
The Journal of biological chemistry |
High |
17462998
|
| 2007 |
RAB11A controls biogenesis of Birbeck granules in Langerhans cells by regulating Langerin trafficking and stability; dominant-negative RAB11A or RAB11A depletion causes missorting of Langerin to lysosomes and abolishes Birbeck granule formation; loss of the RAB11A effector RCP (but not Rip11) also modestly impairs this process, suggesting RAB11A-RCP complexes mediate Langerin recycling. |
Dominant-negative RAB11A overexpression, siRNA depletion of RAB11A and Rab11-FIPs, electron microscopy, fluorescence microscopy |
Molecular biology of the cell |
Medium |
17538027
|
| 2008 |
RAB11A directly interacts with the C-terminal tail of the human prostacyclin receptor (hIP) via a defined 22-amino-acid sequence (Val299-Gln320); this interaction is augmented by agonist stimulation; overexpression of RAB11A increases hIP recycling to the plasma membrane, whereas dominant-negative RAB11A (S25N) impairs recycling. |
Yeast-two-hybrid screen, co-immunoprecipitation in HEK293 cells, dominant-negative RAB11A overexpression, fluorescence co-localization, deletion mapping |
Cellular signalling |
Medium |
18832025
|
| 2008 |
Gβγ subunits interact with RAB11A and co-localize at early and recycling endosomes upon LPA receptor activation; this RAB11A-dependent association promotes PI3K recruitment and AKT phosphorylation at endosomal compartments; dominant-negative RAB11A or RAB11A depletion attenuates LPA-dependent AKT activation and cell survival. |
Co-immunoprecipitation, co-localization, dominant-negative RAB11A expression, siRNA knockdown, AKT phosphorylation assay |
Molecular biology of the cell |
Medium |
18701709
|
| 2008 |
RAB11A is expressed in bladder umbrella cells where it associates with discoidal/fusiform vesicles (DFV); dominant-active RAB11A stimulates apical surface area increase and hGH secretion in the absence of stretch, while dominant-negative RAB11A inhibits stretch-induced exocytosis; endocytosed fluid and membrane markers have little access to RAB11A-positive DFV, suggesting DFV are biosynthetic. |
Adenovirus-mediated dominant-active/dominant-negative RAB11A expression in situ, surface area measurement, secretory marker (hGH) packaging/release assay |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
18843107
|
| 2009 |
RAB11A is required for completion of cytokinesis in Toxoplasma gondii-related apicomplexan parasites; RAB11A associates with Myosin-Tail-Interacting-Protein (MTIP/MLC1), a component of the glideosome motor complex; ablation of RAB11A function results in an incompletely formed Inner Membrane Complex and a block at a late stage of cell division. |
Co-immunoprecipitation (RAB11A-MTIP interaction), dominant-negative RAB11A expression, electron microscopy of IMC formation, conditional knockout |
PLoS pathogens |
Medium |
19165333
|
| 2009 |
RAB11A regulates recycling of extracellular alpha-synuclein from neurons; proteomic analysis of RAB11A-associated proteins identified HSP90, which was validated as a RAB11A-interacting protein; HSP90 inhibition with geldanamycin prevents re-secretion of alpha-synuclein. |
Quantitative proteomics of RAB11A-associated proteins, co-immunoprecipitation of RAB11A-HSP90, alpha-synuclein secretion assay, pharmacological inhibition |
The Journal of neuroscience |
Medium |
19193894
|
| 2009 |
Myosin Vb, RAB11A, and Rab11-FIP2 form a required triple complex for cholesterol-depletion-induced transport of NPC1L1 from the endocytic recycling compartment to the plasma membrane; inactivation of any component of this complex inhibits NPC1L1 export and reduces cellular cholesterol uptake. |
Dominant-negative mutant expression of myosin Vb, RAB11A, and Rab11-FIP2; fluorescence microscopy; cholesterol uptake assay |
The Journal of biological chemistry |
Medium |
19542231
|
| 2010 |
RAB11A controls TLR4 trafficking from the endocytic recycling compartment to E. coli phagosomes; suppression of RAB11A reduces TLR4 and TRAM on phagosomes, inhibiting the IRF3 signaling pathway (IFN-β induction) while NF-κB activation is unaffected. |
siRNA knockdown, co-localization studies, interferon-β reporter assay, NF-κB activity assay |
Immunity |
High |
20933442
|
| 2011 |
RAB11A is indispensable for transport of influenza A vRNPs to the plasma membrane; RAB11A associates with vRNPs at all stages of cytoplasmic transport; siRNA knockdown or expression of dominant-negative/constitutively active RAB11A mutants causes aberrant vRNP perinuclear retention and prevents plasma membrane accumulation; RAB11A-vRNP complex formation was confirmed biochemically. |
siRNA knockdown, dominant-negative/constitutively active RAB11A expression, immunofluorescence, biochemical co-precipitation of RAB11A-vRNP complex |
Journal of virology |
High |
21525351
|
| 2012 |
A RAB11A/Myosin Vb/Rab11-FIP2 platform regulates langerin recycling at two distinct intracellular sites: first at the sorting site in the endosomal recycling compartment (ERC) where transport vesicles are formed, and subsequently at the docking/tethering and fusion step at the plasma membrane. |
Live-FRET, fast FRAP, fast confocal, TIRF microscopy in live cells expressing tagged langerin, RAB11A, Myosin Vb, FIP2 |
Traffic |
Medium |
22420646
|
| 2013 |
RAB11A functions upstream of RAB8A to promote regulated exocytosis of discoidal/fusiform vesicles in bladder umbrella cells; myosin 5B cooperates with the RAB11A-RAB8A module, possibly by facilitating transit through the cortical actin cytoskeleton; Rabin8 (a RAB11A effector and RAB8 GEF) stimulates exocytosis independently of its GEF catalytic activity. |
Dominant-active/dominant-negative RAB11A and RAB8A expression, myosin 5B dominant-negative, catalytically inactive Rabin8 expression, stretch-induced exocytosis assay |
Molecular biology of the cell |
Medium |
23389633
|
| 2013 |
Reggie-1 directly interacts with RAB11A and SNX4; reggie-1 knockdown reduces association of RAB11A with tubular structures and impairs transferrin receptor and E-cadherin recycling to the plasma membrane; these defects are rescued by overexpression of constitutively active RAB11A. |
siRNA knockdown, fluorescence microscopy, co-immunoprecipitation of reggie-1 and RAB11A, transferrin recycling assay, Ca2+-switch E-cadherin recycling assay |
Molecular biology of the cell |
Medium |
23825023
|
| 2013 |
Rab11-FIPs define spatially and temporally distinct regions within the RAB11A-dependent recycling system; internalized transferrin enters different Rab11-FIP-containing compartments with distinct kinetics (FIP1B/FIP2 early; FIP1A/FIP1C/FIP3/FIP5 delayed), indicating temporal ordering of cargo passage through RAB11A recycling subdomains. |
Live-cell deconvolution microscopy, fluorescent transferrin kinetics in HeLa cells expressing chimeric fluorescent Rab11-FIPs |
Molecular biology of the cell |
Medium |
23283983
|
| 2013 |
RAB11A mediates intracellular transport of measles virus RNP complexes in Rab11A-containing recycling endosomes in a microtubule-dependent manner; dominant-negative RAB11A severely impairs RNP apical accumulation and infectious virion shedding from polarized epithelial cells. |
Live-cell imaging with fluorescent protein-tagged L protein, dominant-negative RAB11A expression, nocodazole treatment, viral titer assay |
Journal of virology |
Medium |
23408617
|
| 2014 |
TBC1D9B acts as a GAP for RAB11A in polarized MDCK cells; TBC1D9B interacts with RAB11A in a nucleotide-dependent manner via its TBC domain and specifically stimulates GTP hydrolysis on RAB11A (but not other Rabs tested at physiological Mg2+); TBC1D9B overexpression decreases active RAB11A, disrupts the RAB11A-Sec15A interaction, and slows IgA transcytosis, while TBC1D9B knockdown accelerates it. |
GTPase activity assay in vitro, co-immunoprecipitation, overexpression and shRNA knockdown of TBC1D9B, IgA transcytosis assay, active RAB11A pull-down |
Molecular biology of the cell |
High |
25232007
|
| 2014 |
Rab11-FIP2 interacts with MYO5B via residues S229 and G233; mutations disrupting this interaction increase speed and track length of RAB11A-containing vesicle movement, consistent with impaired MYO5B-mediated tethering; Rab11-FIP2 knockdown phenocopies this. |
Random mutagenesis, yeast two-hybrid, HeLa cell expression assays, live-cell fluorescence microscopy of RAB11A vesicle dynamics |
Traffic |
Medium |
24372966
|
| 2014 |
RAB11A is required for apical protein localization in mouse intestinal epithelial cells in vivo; intestine-specific RAB11A knockout mice show apical protein mislocalization to the basolateral membrane, shortened microvilli, and microvillus inclusion bodies; RAB8A mislocalizes in RAB11A knockout intestine, and RAB11A mislocalizes in RAB8A knockout intestine, indicating a functional relationship between RAB11A, RAB8A, and myosin Vb. |
Conditional knockout mouse, immunofluorescence, electron microscopy, epistasis analysis with RAB8A knockout |
Biology open |
High |
25527643
|
| 2014 |
Loss of RAB11A in mouse embryonic fibroblasts impairs secretion of multiple soluble matrix metalloproteinases (MMPs); global RAB11A knockout embryos form normal blastocysts but die at peri-implantation stages. |
Global RAB11A knockout mouse, multiple trafficking assays, MMP secretion assays, complementation analysis |
The Journal of biological chemistry |
Medium |
25271168
|
| 2014 |
RAB11A deficiency in enterocytes alters apical localization of syntaxin 3 and impairs microvillus assembly; conditional RAB11A knockout mice and stable RAB11A-knockdown CaCo2-BBE cells both show shortened or displaced microvilli, affirming RAB11A's role in apical membrane trafficking in intestinal cells. |
Conditional knockout mouse, stable shRNA knockdown, immunofluorescence, electron microscopy |
Journal of cell science |
Medium |
25673875
|
| 2014 |
Myosin Vb and RAB11A control phosphorylation of ezrin at T567 in enterocytes; dominant-negative RAB11A or myosin Vb depletion prevents subapical enrichment of RAB11A and ezrin kinases and reduces ezrin phosphorylation and microvilli development; similar loss occurs in microvillus inclusion disease (MYO5B mutations). |
Dominant-negative RAB11A expression, myosin Vb knockdown, phospho-specific ezrin western blot, immunofluorescence |
Journal of cell science |
Medium |
24413175
|
| 2014 |
MYO5B uncoupling from RAB11A induces microvillus inclusions in enterocytes; the MVID-associated MYO5B-P660L mutation loses interaction with RAB11A and causes microvillus inclusion formation; microvilli restoration requires RAB8A-MYO5B interaction, while microvillus inclusions are driven by loss of RAB11A-MYO5B interaction; early inclusions are SNX18-positive and derived from apical membrane internalization. |
Stable MYO5B knockdown in CaCo2-BBE cells, expression of WT and mutant MYO5B, surface biotinylation, immunofluorescence, co-immunoprecipitation |
The Journal of clinical investigation |
High |
24892806
|
| 2015 |
RAB11A and Rab11-FIP2 mediate VE-cadherin recycling and vascular barrier integrity; VE-cadherin directly interacts with Rab11-FIP2 (at aa 453-484), forming a ternary complex with RAB11A; silencing RAB11A or Rab11-FIP2 prevents VE-cadherin recycling and junctional reannealing; selective pulmonary microvessel RAB11A knockdown increases vascular leakage in sepsis models. |
Yeast two-hybrid, co-immunoprecipitation, Ca2+-switch recycling assay, confocal imaging, siRNA knockdown, in vivo intratracheal siRNA, permeability assay |
Arteriosclerosis, thrombosis, and vascular biology |
High |
26663395
|
| 2015 |
RAB11A inactivation in macrophages facilitates efferocytosis of apoptotic neutrophils via modulation of ADAM17-mediated CD36 surface expression; apoptotic cell feeding induces rapid loss of RAB11A activity; RAB11A knockdown increases surface CD36 by reducing ADAM17 surface levels; blockade of CD36 abolishes the augmented phagocytosis. |
siRNA knockdown, wild-type and dominant-negative RAB11A overexpression, flow cytometry for surface CD36/ADAM17, efferocytosis assay, in vivo instillation of RAB11A-depleted macrophages |
Journal of immunology |
Medium |
28053235
|
| 2015 |
Huntingtin (HTT) forms a complex with PAR3, aPKC, and RAB11A, and ensures microtubule-dependent apical vesicular translocation of PAR3-aPKC through RAB11A; HTT depletion disrupts apical localization of PAR3-aPKC during mammary epithelial morphogenesis. |
Co-immunoprecipitation (HTT-PAR3-aPKC-RAB11A complex), conditional HTT depletion in vivo, immunofluorescence, mouse mammary epithelium model |
PLoS biology |
Medium |
25942483
|
| 2015 |
RAB11A is essential for lamellar body biogenesis in human epidermis; RAB11A silencing in 3D reconstructed human epidermis reduces lamellar body density and secretion, misdirects lamellar body cargoes to lysosomes, decreases stratum corneum lipid content, and causes epidermal barrier defects. |
siRNA knockdown in 3D reconstructed human epidermis, electron microscopy, immunofluorescence, epidermal barrier function assay |
The Journal of investigative dermatology |
Medium |
26872604
|
| 2016 |
RAB11A regulates ezrin phosphorylation and microvilli-associated membrane supply in neurons via LMTK1; LMTK1 knockout increases prevalence, velocity, and run length of anterograde RAB11A-positive endosome movement; a non-phosphorylatable LMTK1 mutant at Ser34 (Cdk5 phosphorylation site) dramatically promotes dendrite growth; Cdk5-LMTK1 axis negatively controls dendritic formation through regulation of RAB11A-positive endosomal trafficking. |
LMTK1 knockout mice, live-cell imaging of RAB11A-positive endosome dynamics, dominant-negative and constitutively active RAB11A expression, in vitro and in vivo cortical neuron cultures |
Molecular biology of the cell |
Medium |
24672056
|
| 2017 |
ET-1 activates PKC, which phosphorylates RAB11A at serine 177, inhibiting RAB11A activity and reducing surface trafficking of BK channel β1 subunits in arterial smooth muscle cells; expression of phosphorylation-incapable RAB11A S177A blocks ET-1-induced effects; NO-induced RAB11A activation and vasodilation do not involve S177. |
PKC inhibitor, RAB11A S177A phosphorylation-incapable mutant expression, RAB11A activity assay, surface protein quantitation, patch-clamp electrophysiology, ex vivo vasoconstriction assay |
Circulation research |
High |
28696251
|
| 2017 |
RAB11A promotes proliferation and invasion in non-small cell lung cancer via interaction with and upregulation of YAP protein; co-immunoprecipitation shows RAB11A-YAP interaction in lung cancer cells; YAP depletion abolishes RAB11A-induced cell cycle protein changes and proliferation. |
Co-immunoprecipitation, RAB11A overexpression/knockdown, YAP siRNA epistasis, cell proliferation and invasion assays |
Oncotarget |
Low |
28468127
|
| 2018 |
RAB11A-positive recycling endosomes serve as a primary platform for autophagosome biogenesis; WIPI2 is recruited to RAB11A-positive membranes by binding RAB11A, and PI3P is generated on these membranes upon starvation; loss of RAB11A impairs recruitment and assembly of the autophagic machinery including WIPI2, ATG16L1, and LC3. |
RAB11A knockout/knockdown, confocal and live-cell imaging, WIPI2-RAB11A binding assay, PI3P detection on RAB11A membranes, LC3 lipidation assay, mitophagy and transferrin receptor autophagy assays |
Developmental cell |
High |
29634932
|
| 2018 |
Rab11a and Rab8a act in a cascade (RAB11A upstream of RAB8A, independent of Rabin8 GEF activity) to regulate tunneling nanotube (TNT) formation; overexpression of both increases TNT-connected cells and intercellular vesicle propagation; VAMP3 acts downstream of RAB8A in this pathway. |
RAB11A and RAB8A overexpression/dominant-negative expression, Rabin8 catalytic mutant, live-cell imaging, TNT quantification, VAMP3 interference |
Journal of cell science |
Medium |
30209134
|
| 2019 |
The LMTK1A-TBC1D9B-RAB11A cascade regulates dendritic spine formation; LMTK1 binds and controls the GAP activity of TBC1D9B on RAB11A; TBC1D9B inactivates RAB11A under LMTK1A control; depletion of LMTK1 or TBC1D9B increases spine formation and density in neurons in vitro and in vivo. |
Co-immunoprecipitation (LMTK1-TBC1D9B), in vitro GAP assay, siRNA/shRNA knockdown in primary neurons and in vivo mouse brain, spine density analysis by confocal microscopy |
The Journal of neuroscience |
High |
31628178
|
| 2019 |
Myosin-5b motor function is activated by RAB11A binding to its globular tail domain (GTD), which abolishes the autoinhibitory head-GTD interaction; FIP2 bridges MYO5B and RAB11A on vesicles without directly activating the motor; RAB11A has higher affinity for FIP2 than for MYO5B, suggesting FIP2-mediated vesicle tethering with RAB11A-dependent motor activation. |
In vitro binding assays (RAB11A-MYO5B GTD interaction), ATPase/motor activity assay, affinity measurements |
Bioscience reports |
Medium |
30545898
|
| 2020 |
The C9ORF72-SMCR8-WDR41 complex has GAP activity toward RAB11A and RAB8A; cryo-EM structure at 3.2 Å reveals that Arg147 of SMCR8 acts as the arginine finger critical for stimulating GTP hydrolysis by RAB11A; biochemical mutagenesis of R147 eliminates this GAP activity. |
Cryo-EM structure determination, in vitro GTPase activity assay with SMCR8 R147 mutant, biochemical analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
32303654
|
| 2020 |
RAB11A is directly activated (GTP-loaded) by the insulin signaling cascade in a PI3K- and Akt-dependent manner; GTP loading of RAB11A peaks ~4 min after insulin stimulation and is required for GLUT4 and FAT/CD36 trafficking in cardiomyocytes. |
Biotinylated GTP analog loading assay, PI3K/Akt inhibitor pharmacology, siRNA knockdown in H9c2-hIR cells |
Cellular signalling |
Medium |
17158030
|
| 2020 |
RAB11A Rab11A-positive vesicles serve as hubs for congregation of influenza vRNP complexes, enabling vRNP:vRNP interactions required for specific genome assembly; RAB11A-deficient cells produce smaller vRNP bundles with reduced co-localization between distinct vRNA segments and generate non-infectious particles with high RNA copy-to-PFU ratios. |
Tetracysteine-tagged NP reporter virus, siRNA RAB11A depletion, fluorescence microscopy of vRNP dynamics, RNA copy number/PFU ratio assay |
PLoS pathogens |
Medium |
33970958
|
| 2020 |
IAV infection decreases speed and increases arrest of RAB11A-positive recycling endosomes through a mechanism involving reduced dynein motor association with RAB11A vesicles; co-transport of RAB11A and vRNA was directly demonstrated in infected cells by two-color live imaging. |
High-spatiotemporal-resolution light-sheet microscopy, two-color live imaging, quantitative motion analysis, proteomic analysis of dynein association |
Nature communications |
Medium |
31911620
|
| 2021 |
RAB11A mediates cell-cell spread of influenza A vRNPs via tunneling nanotubes (TNTs); in a system where conventional virion-mediated spread was blocked, vRNP transfer to neighboring cells was dependent on both actin and RAB11A; genome mixing and reassortment via TNT transfer was demonstrated. |
HA-deficient reporter virus system, actin disruption, RAB11A knockdown/dominant-negative, fluorescence microscopy of TNTs, infectious virus reassortment assay |
PLoS pathogens |
Medium |
34473799
|
| 2021 |
RAB11A controls YAP localization to adherens and tight junctions in colonic epithelium; loss of RAB11A reduces YAP association with α-catenin, β-catenin, and Merlin, and causes nuclear YAP accumulation and increased β-catenin-YAP complex formation; RAB11A-deficient mice show reduced colonic epithelial integrity and impaired repair after chemical injury. |
Conditional RAB11A knockout mice, co-immunoprecipitation (YAP with junctional components), immunofluorescence, epithelial injury assay |
The Journal of biological chemistry |
Medium |
34058200
|
| 2022 |
The C-terminal two-thirds of the influenza A virus PB2 polymerase subunit (PB2-C, comprising cap-binding, mid-link, 627, and NLS domains) directly interact with RAB11A; SAXS confirms a compact 1:1 stoichiometric complex in solution; the switch I region of RAB11A (used for Rab11-FIP binding) mediates PB2-C binding, indicating competition between viral polymerase and Rab11-FIPs for the same RAB11A site. |
Pulldown assays, mass spectrometry, small-angle X-ray scattering (SAXS), domain deletion mapping |
Journal of virology |
High |
35019720
|
| 2023 |
RAB11A and RAB11B redundantly control mitotic spindle function in intestinal epithelial progenitor cells; compound RAB11A/RAB11B double-knockout causes mitotic spindle defects, cell cycle arrest, and apoptosis leading to lethality within 3 days; unbiased proteomics of RAB11A and RAB11B immunoprecipitates identified shared mitotic spindle microtubule regulators; disrupting RAB11 impairs KIF11 (kinesin motor) function and bipolar spindle formation. |
Double-knockout mouse model, enteroid culture, proteomic immunoprecipitation, KIF11 functional analysis, mitotic spindle imaging |
EMBO reports |
High |
37424454
|
| 2023 |
Accessory ESCRT-III proteins CHMP1A, CHMP1B, CHMP5, and IST1 are selectively required for ILV formation in RAB11A-positive recycling endosomes but not in late endosomes; CHMP5 knockdown in HCT116 cells selectively inhibits RAB11A-exosome production without affecting late-endosome-derived exosomes. |
Comparative proteomics, Drosophila secondary cell knockdown, human HCT116 cell siRNA knockdown, electron microscopy of ILVs, exosome secretion assay |
Journal of extracellular vesicles |
Medium |
36872252
|
| 2018 |
FLCN (folliculin, Birt-Hogg-Dubé protein) binds RAB11A via its C-terminal DENN-like domain; suppression of either RAB11A or FLCN redirects overexpressed PAT1 (amino acid transporter) to lysosomes and reduces its plasma membrane targeting; FLCN promotes loading of PAT1 onto RAB11A vesicles; FLCN does not have direct GEF activity on RAB11A in vitro. |
Co-immunoprecipitation of FLCN-RAB11A, in vitro GEF activity assay (negative result for FLCN), siRNA knockdown, PAT1 trafficking assay |
Journal of cell science |
Medium |
30446510
|
| 2014 |
Rab11a-Rab8a double-knockout in neonatal enterocytes causes basolateral microvilli formation and more severe enteropathy than either single knockout; inducible Rab11a deletion alone from neonatal enterocytes induces basolateral microvilli within 3 days; distinct cargo sets depend individually on Rab8a or Rab11a, while some basolateral cargos are redundantly transported by both. |
Enterocyte-specific single and double conditional knockout mice, inducible Rab11a deletion, immunofluorescence, electron microscopy |
Journal of cell science |
High |
28596241
|