| 1993 |
RAB17 is a small GTPase specific to epithelial cells, induced upon mesenchymal-to-epithelial differentiation during kidney development, and localizes to the basolateral plasma membrane and apical tubules, suggesting a role in transcellular transport. |
Northern blot, in situ hybridization, immunofluorescence, immunoelectron microscopy on mouse kidney sections |
The Journal of cell biology |
Medium |
8486736
|
| 1998 |
RAB17 associates with the apical recycling endosome in polarized Eph4 epithelial cells and with the perinuclear recycling endosome in non-polarized BHK-21 cells; dominant-negative (GTP-binding deficient) and constitutively active (hydrolysis-deficient) RAB17 mutants specifically increased basolateral-to-apical transcytosis of transferrin receptor and FcLR chimeric receptor, and stimulated apical recycling, establishing RAB17 as a regulator of traffic through the apical recycling endosome. |
Confocal immunofluorescence microscopy, expression of GTPase mutants, transcytosis assays in polarized Eph4 cells |
The Journal of cell biology |
High |
9490718
|
| 1998 |
RAB17 localizes to small vesicles and tubules in the apical region of MDCK cells, colocalizes with dimeric IgA internalized via the polymeric immunoglobulin receptor (pIgR) from both apical and basolateral surfaces, and overexpression of RAB17 impairs basolateral-to-apical transcytosis of dimeric IgA, providing morphological and functional evidence for RAB17 in regulating transcellular traffic through apical recycling endosomes. |
Stable MDCK cell lines expressing wild-type or mutant RAB17 and pIgR, immunofluorescence/electron microscopy, IgA transcytosis assay |
The Journal of biological chemistry |
High |
9624171
|
| 1999 |
RAB17 colocalizes with IgA along the basolateral plasma membrane and in basolateral endosomes/vesicles of mouse enterocytes, supporting its involvement in IgA transcytosis through raft-containing compartments in vivo. |
Immunogold electron microscopy on mouse small intestinal explants |
Gastroenterology |
Medium |
10029620
|
| 2011 |
RAB17 localizes to recycling endosomes and melanosomes in melanocytic cells; siRNA knockdown of RAB17 causes accumulation of melanosomes at the cell periphery and increased melanin retention inside cells, inhibits filopodia formation, and acts downstream of RAB27a in the melanosome release pathway. |
GFP-RAB17 live imaging, siRNA knockdown, double knockdown with RAB27a, melanin quantification, filopodia counting in melanoma cells |
Traffic |
Medium |
21291502
|
| 2012 |
RAB17 localizes specifically to dendritic growth cones, shafts, filopodia, and mature spines (but not axons) in mouse hippocampal neurons; shRNA-mediated knockdown reduces dendrite growth, branching, and dendritic spine number, identifying RAB17 as a regulator of dendrite-specific membrane trafficking and postsynaptic development. |
shRNA knockdown, immunofluorescence, morphometric analysis in mouse hippocampal neurons |
The Journal of biological chemistry |
Medium |
22291024
|
| 2012 |
ERK2 (but not ERK1) suppresses RAB17 gene expression, and knockdown of RAB17 restores invasive migration in ERK2-depleted MDA-MB-231 cancer cells, placing RAB17 downstream of ERK2 as an inhibitor of invasive migration in 3D matrices. |
ERK2 siRNA knockdown, gene expression arrays, RAB17 siRNA knockdown in ERK2-depleted cells, 3D invasion assays |
Journal of cell science |
Medium |
22328529
|
| 2013 |
Rabex-5 (a Rab5-GEF) interacts with a GDP-locked RAB17 mutant and promotes translocation of RAB17 from the cell body to the dendrites of developing mouse hippocampal neurons; shRNA knockdown of Rabex-5 inhibits both axon and dendrite morphogenesis, while RAB17 knockdown affects dendrite morphogenesis alone, indicating Rabex-5 acts upstream of RAB17 as its GEF to regulate dendritogenesis. |
Yeast two-hybrid screen with GDP-locked RAB17 as bait, shRNA knockdown, live-cell fluorescence imaging in mouse hippocampal neurons |
The Journal of biological chemistry |
Medium |
23430262
|
| 2014 |
RAB17 knockdown reduces surface expression of the kainate receptor subunit GluK2, but not AMPA receptor subunit GluA1; RAB17 colocalizes with Syntaxin-4 in dendrites, and RAB17 knockdown causes Syntaxin-4 redistribution from dendrites to axons; constitutively active RAB17 promotes dendritic GluK2 surface expression by enhancing Syntaxin-4 translocation to dendrites, indicating RAB17 selectively regulates KAR surface expression by mediating dendritic trafficking of Syntaxin-4. |
shRNA knockdown, surface biotinylation, immunofluorescence, overexpression of constitutively active RAB17 in rat hippocampal neurons |
The Journal of biological chemistry |
Medium |
24895134
|
| 2014 |
RAB17-mediated recycling endosomes supply membrane to Group A Streptococcus-containing autophagosome-like vacuoles (GcAVs); dominant-negative RAB17 (N132I) reduces GcAV formation efficiency, while RAB17 overexpression increases TfR-positive GcAV content; knockdown of upstream activator Rabex-5 similarly reduces GcAV formation, establishing RAB17 as a mediator of recycling endosome-to-autophagosome membrane supply during antibacterial autophagy. |
Colocalization analysis, dominant-negative overexpression, siRNA knockdown, Rabex-5 knockdown in GAS-infected cells |
Cellular microbiology |
Medium |
25052408
|
| 2016 |
Mass spectrometry of efferosomes in macrophages showed that they lack antigen presentation proteins and instead recruit RAB17; RAB17-dependent sorting diverts efferocytosed cargo away from the MHC class II loading compartment via the recycling endosome pathway, preventing presentation of apoptotic cell-derived antigens. |
Mass spectrometry, immunofluorescence microscopy of efferosomes vs phagosomes, functional antigen presentation assays in macrophages |
Cell death & disease |
Medium |
28005073
|
| 2016 |
RAB17 undergoes monosumoylation (shifting from 25 kDa to 40 kDa), and prenylation is required for sumoylation; the GTP-bound, sumoylated form of RAB17 selectively binds Syntaxin-2 (but not Syntaxins 3 or 4) in polarized hepatic WIF-B cells; a sumoylation-deficient K68R mutant redistributes Syntaxin-2 and 5'-nucleotidase from the apical membrane to subapical puncta, indicating sumoylation-dependent interactions with Syntaxin-2 mediate apical vesicle fusion. |
Recombinant adenovirus expression, immunoblotting, co-immunoprecipitation, mutant analysis (K68R, GTP/GDP-bound forms) in polarized WIF-B cells |
The Journal of biological chemistry |
High |
26957544
|
| 2017 |
RAB17 is rapidly recruited to efferosomes after apoptotic cell uptake; efferosomes migrate to the cell center where they undergo RAB17-dependent vesiculation, and resulting vesicles traffic in a RAB17-dependent manner to the cell periphery, transferring cargo to recycling endosomes to prevent further phagolysosome maturation. |
Live-cell imaging, immunofluorescence microscopy, RAB17 functional perturbation in macrophages |
Small GTPases |
Medium |
28471261
|
| 2018 |
RAB17 regulates basolateral-to-apical transcytotic vesicle docking and fusion at the apical surface in polarized hepatic WIF-B cells; GTP-bound and sumoylated RAB17 are required for apical vesicle docking; GTP hydrolysis is required for vesicle delivery; transcytosis is impaired at the subapical compartment-to-apical surface step; this function applies broadly to three classes of newly synthesized apical residents. |
Exogenous expression of wild-type, dominant active, dominant negative, and sumoylation-deficient RAB17 in polarized WIF-B hepatocytes; transcytosis assays; immunofluorescence |
Molecular biology of the cell |
High |
30256711
|
| 2019 |
Influenza A virus HA and NA colocalize with RAB17-positive compartments after synthesis; dominant-negative RAB17 significantly delays HA transport to the plasma membrane; HA associates with RAB17 in lipid raft fractions by co-immunoprecipitation; cholesterol depletion by methyl-β-cyclodextrin abolishes RAB17-associated NA movement, indicating RAB17 mediates cholesterol/lipid raft-dependent apical transport of viral envelope proteins. |
Confocal microscopy in stable AcGFP-Rab cell lines, dominant-negative RAB17 expression, co-immunoprecipitation from lipid raft fractions, methyl-β-cyclodextrin treatment, live-cell imaging |
Frontiers in microbiology |
Medium |
31456775
|
| 2020 |
ALS2 interacts physically with RAB17 but lacks GEF activity for RAB17 (RABGEF1/Rabex-5 is the actual Rab17-GEF); ALS2 acts downstream of RABGEF1 and regulates maturation of Rab17-residing nascent endosomes to EEA1-positive early endosomes; upon Rac1 activation, RAB17 and ALS2 are co-recruited to membrane ruffles and early endosomes in a Rab5-activity-independent manner; RAB17 localization to recycling endosomes depends on RAB11 expression. |
Co-immunoprecipitation, GEF activity assays, shRNA knockdown, Rac1 activation, immunofluorescence in cell lines |
Biochemical and biophysical research communications |
Medium |
31959474
|
| 2024 |
RAB17 attenuates ferroptosis in endometrial cancer cells by inhibiting transferrin receptor (TFRC) protein expression through a ubiquitin proteasome-dependent mechanism; RAB17 expression is increased under low-glucose conditions and limits ferroptosis to promote cancer cell survival via the RAB17-TFRC axis. |
RAB17 overexpression/knockdown, western blot for TFRC, proteasome inhibitor assays, in vitro and in vivo xenograft models |
Cell death & disease |
Medium |
39242574
|
| 2025 |
LMO4 promotes ubiquitin-proteasome-dependent degradation of RAB17 in oral squamous cell carcinoma cells; restoration of RAB17 expression reduces proliferation, migration, and ferroptosis resistance conferred by LMO4, identifying LMO4 as an upstream E3 ligase-recruiting factor that negatively regulates RAB17 protein levels post-translationally. |
LMO4 overexpression/knockdown, RAB17 rescue expression, western blot, proteasome inhibitor assays, xenograft mouse model |
Cell death & disease |
Medium |
41213908
|
| 2025 |
RAB17 expression in hepatoma-derived Clone 9 cells induces actin- and cholesterol-dependent lateral membrane protrusions in a GTP-dependent manner; RAB17 selectively redistributes invadopodia proteins to protrusion tips and reduces matrix degradation; RAB17 interacts with MAL2 in a GTP-dependent manner; RAB17 redirects newly synthesized membrane proteins from the Golgi to induced protrusions in a GTP-dependent manner. |
Exogenous expression of wild-type and GTPase mutants, co-immunoprecipitation, actin/cholesterol depletion, matrix degradation assays, live trafficking assays in Clone 9 cells |
Molecular biology of the cell |
Medium |
39813085
|