| 2015 |
Rab26 (GTP-bound/active form) specifically associates with clusters of synaptic vesicles in neurites and directs synaptic and secretory vesicles into preautophagosomal structures co-localizing with Atg16L1, LC3B, and Rab33B. Atg16L1 was identified as a direct effector of Rab26, binding selectively to the GTP-bound form of Rab26. |
Overexpression of active vs. GDP-preferring Rab26 mutants in neurons, co-localization with autophagy markers, direct binding assay (Atg16L1 as effector) |
eLife |
High |
25643395
|
| 2009 |
RAB26 is a direct transcriptional target of the transcription factor MIST1, which binds conserved CATATG E-boxes in the RAB26 promoter to activate its transcription. RAB26 activity (alongside RAB3D) is required for the formation of large secretory granules in gastric zymogenic cells; dominant-negative RAB26 and RAB prenylation inhibitors abrogate granule formation. |
ChIP/EMSA showing MIST1 binding to RAB26 E-boxes; dominant-negative RAB26 transfection; RAB prenylation inhibitor treatment; RFP-pepsinogen C granule formation assay |
Molecular and cellular biology |
High |
20038531
|
| 2000 |
Rab26 protein localizes specifically to secretory granule membranes in parotid acinar cells, binds GTP, and its immunostaining disappears after isoproterenol treatment, consistent with a role in regulated secretory granule exocytosis. |
Western blotting with GTP-binding assay ([α-32P]GTP), subcellular fractionation, immunocytochemistry (light and electron microscopy) |
Histochemistry and cell biology |
Medium |
10857477
|
| 2005 |
Rab26 localizes to mature (not immature) secretory granule membranes in parotid acinar cells. Anti-Rab26 antibody inhibits isoproterenol (β-adrenergic/cAMP)-induced amylase release from permeabilized acinar cells but has no effect on Ca2+-induced amylase release, indicating a selective role in cAMP-dependent granule recruitment to the plasma membrane. |
Percoll-sucrose density gradient fractionation; antibody inhibition of exocytosis in streptolysin-O-permeabilized acinar cells; amylase secretion assay |
Archives of oral biology |
Medium |
16076461
|
| 2012 |
Rab26 regulates anterograde transport of α2A- and α2B-adrenergic receptors from the Golgi to the cell surface. Rab26 mutants and siRNA-mediated knockdown arrest receptors in the Golgi and reduce cell surface receptor numbers. Rab26 directly and activation-dependently interacts with the third intracellular loop of α2B-AR. |
Rab26 mutant overexpression and siRNA knockdown; cell surface receptor quantification; co-immunoprecipitation/pulldown demonstrating direct GTP-dependent interaction with α2B-AR third intracellular loop |
The Journal of biological chemistry |
High |
23105096
|
| 2014 |
RAB26 associates predominantly with LAMP1/cathepsin D-positive lysosomes (not secretory granules) and drives lysosome coalescence into a central perinuclear region. Lysosome clustering caused by increased RAB26 expression in turn redistributes mitochondria into distinct subcellular neighborhoods. |
Fluorescence co-localization with lysosomal and secretory granule markers; induction of zymogen-secreting cell differentiation; direct transfection of RAB26 |
Journal of cell science |
Medium |
24413166
|
| 2018 |
RAB26 promotes autophagic degradation of phosphorylated (active) SRC kinase in endothelial cells through direct, GTP-dependent interaction with ATG16L1. Loss of RAB26 leads to SRC phosphorylation, CDH5/VE-cadherin phosphorylation, CDH5 internalization, and disruption of adherens junctions, increasing vascular permeability in acute lung injury. |
RAB26 knockout mice (vascular permeability assays), siRNA depletion and overexpression in HPMECs, co-immunoprecipitation of RAB26 with ATG16L1 (GTP-dependent), western blot for phospho-SRC and phospho-CDH5 |
Autophagy |
High |
29965781
|
| 2019 |
RAB26 is a critical target of SNRPB-mediated splicing regulation in NSCLC; SNRPB depletion causes intron 7 retention in RAB26 mRNA, triggering nonsense-mediated decay (NMD) and reducing RAB26 protein levels. Forced RAB26 re-expression partially rescues decreased tumorigenicity caused by SNRPB depletion. |
siRNA knockdown of SNRPB; RT-PCR demonstrating intron retention; NMD pathway analysis; RAB26 re-expression rescue assay |
Cell death & disease |
Medium |
31511502
|
| 2020 |
The Coxiella burnetii effector protein CvpF specifically interacts with host RAB26, recruiting the autophagosomal marker LC3B to Coxiella-containing vacuoles, thereby subverting RAB26-dependent autophagy to promote vacuole biogenesis and bacterial virulence. |
Transposon mutant library screen; co-immunoprecipitation/pulldown of CvpF with RAB26; LC3B recruitment assay; SCID mouse virulence model |
Autophagy |
Medium |
32116095
|
| 2021 |
Rab26 mediates autophagic degradation of phosphorylated Src kinase in breast cancer cells through interaction with ATG16L1. Rab26 promotes endosomal translocation of Src and reduces Src at focal adhesions, thereby suppressing cell migration and invasion. |
Rab26 overexpression and knockdown; immunofluorescence co-localization of Src with endosomal markers; Co-IP with ATG16L1; migration/invasion assays |
Cell death & disease |
Medium |
33731709
|
| 2021 |
Rab26 regulates cell surface transport of the erythropoietin receptor (EPOR) in macrophages; loss of Rab26 reduces surface EPOR levels, impairs EPO-mediated M2 macrophage polarization, and tips macrophage phenotype toward M1. |
Rab26 KO mice; macrophage polarization assays; cell surface EPOR measurement after Rab26 modulation |
Frontiers in immunology |
Medium |
34925338
|
| 2022 |
SMAD3 transcriptionally activates RAB26 by binding to the RAB26 promoter, as demonstrated by dual-luciferase reporter and chromatin immunoprecipitation assays. SMAD3 overexpression blocks inhibitory effects of RAB26 silencing on NSCLC cell proliferation, migration, and invasion. |
Dual-luciferase reporter assay; chromatin immunoprecipitation (ChIP); RAB26 shRNA knockdown; SMAD3 overexpression rescue |
Bioengineered |
Medium |
35291909
|
| 2022 |
In Drosophila salivary glands, Rab26 localizes to immature secretory glue granules and prevents their acidification and premature maturation. Rab26 loss accelerates granule maturation, acidification, fusion, and lysosomal breakdown (crinophagy). Loss of Mon1 (an activator of Rab7) causes Rab26 to remain on large granules, implicating a Mon1-Rab7 pathway that counteracts Rab26 to drive granule maturation. |
Rab26 mutant Drosophila; fluorescence microscopy of glue granule acidification and fusion; genetic epistasis with Mon1 mutant; overexpression studies |
Cellular and molecular life sciences |
Medium |
36600084
|
| 2022 |
Manganese-induced α-synuclein overexpression suppresses Rab26-ATG16L1 co-localization and reduces LC3II-positive synaptic vesicles, impairing Rab26-dependent autophagy initiation and causing accumulation of dysfunctional synaptic vesicles. Knockdown of α-synuclein with shRNA restores Rab26-ATG16L1 co-localization in Mn-exposed neurons. |
α-synuclein shRNA knockdown in primary hippocampal neurons; co-localization of Rab26 with ATG16L1 and LC3II-positive SVs by immunofluorescence; in vivo Mn exposure mouse model |
The Science of the total environment |
Medium |
36341850
|
| 2023 |
Rab26 directly interacts with synaptotagmin-1 (Syt1) via the Syt1 C2A domain (shown by GST pulldown), interfering with Syt1-SNAP25 interaction and inhibiting exocytosis of newcomer insulin granules. Rab26 knockout mice show increased glucose-stimulated insulin secretion, and Rab26 overexpression in islets suppresses insulin secretion; Rab26 overexpression causes clustering of insulin granules. |
Rab26-/- mice (CRISPR/Cas9); GST pulldown of Rab26 with Syt1 C2A domain; TIRF microscopy of insulin granule exocytosis; Rab26 KD in insulinoma cells; islet transplantation assay |
PLoS biology |
High |
37289842
|
| 2023 |
Rab26 interacts with mitochondrial fusion protein MFN2 and regulates MFN2 transport to mitochondria. Rab26 deficiency reduces mitochondrial MFN2 levels, decreases mitochondrial ROS and ATP production, and impairs macrophage phagocytosis and bacterial clearance. |
Co-immunoprecipitation of Rab26 with MFN2; Rab26 KO bone marrow-derived macrophages; MFN2 siRNA knockdown; mitochondrial ROS and ATP measurement; phagocytosis/bacterial killing assays; in vivo ARDS mouse model |
The FEBS journal |
Medium |
37060270
|
| 2023 |
KLF4 transcriptionally targets RAB26 (verified by luciferase reporter assay) to inhibit autophagy in colon cancer cells. KLF4 overexpression suppresses LC3II/I ratio and autophagosome formation; RAB26 knockdown or rapamycin treatment reverses this effect and restores 5-FU resistance. |
Luciferase reporter assay for KLF4-RAB26 promoter interaction; RAB26 shRNA knockdown; autophagosome imaging by confocal microscopy; 5-FU resistance assay; xenograft mouse model |
Cancer biology & therapy |
Medium |
37431852
|
| 2023 |
ROS/cigarette smoke exposure induces DNMT3b-mediated hypermethylation of the Rab26 promoter, suppressing Rab26 expression. Reduced Rab26 activates p38 and JNK MAPK signaling to promote airway epithelial inflammatory mediator production; Rab26 overexpression attenuates this response. |
Rab26 promoter methylation assay; DNMT3b siRNA; antioxidant (NAC) and DNA methylation inhibitor (5-AZA) treatment; Rab26 overexpression/silencing with p38/JNK phosphorylation readouts; in vivo smoking mouse model |
Free radical biology & medicine |
Medium |
36610560
|
| 2025 |
Rab26 interacts with angiotensin II Type 1 receptor (AT1R) and promotes its transport to the cell surface in pulmonary artery smooth muscle cells (PASMCs), thereby activating STAT3 and upregulating/promoting nuclear translocation of YAP1, driving PASMC hyper-proliferation under hypoxia. |
Co-immunoprecipitation of Rab26 with AT1R; Rab26 KO mice (PAH model); pharmacological inhibition of AT1R and pSTAT3; assessment of pSTAT3 and YAP1 levels; pulmonary vascular remodeling histology |
Cellular and molecular life sciences |
Medium |
41231254
|
| 2025 |
Rab26 deficiency in mice causes depression/anxiety-like behaviors and cognitive impairment. Mechanistically, Rab26 interacts with the serotonin transporter SERT and promotes its autophagic degradation; loss of Rab26 increases cell surface SERT levels, reduces synaptic vesicle turnover (accumulation of SVs at presynaptic terminals), and decreases mEPSC frequency and LTP. |
Rab26-/- mice; behavioral tests; co-immunoprecipitation of Rab26 with SERT; cell surface SERT measurement; electrophysiology (mEPSC, LTP); electron microscopy of SV accumulation |
iScience |
Medium |
40687824
|
| 2025 |
Rab26 facilitates lysosomal translocation and degradation of eukaryotic elongation factor 1A (eEF1A) in cardiomyocytes. Cardiac-specific Rab26 overexpression (via AAV9) reduces eEF1A levels, improving cardiac function and reducing hypertrophy; eEF1A silencing eliminates the cardioprotective effect of Rab26. |
Protein interaction studies (Co-IP/pulldown); fluorescence co-localization of Rab26 and eEF1A with lysosomes; protease inhibition assays; AAV9-cardiac-specific Rab26 overexpression; Rab26 KO; TAC mouse model |
Life sciences |
Medium |
40609824
|
| 2026 |
Rab26 physically binds to mitochondrial VDAC1 and prevents its oligomerization. Loss of Rab26 promotes VDAC1 oligomerization, mitochondrial membrane permeabilization, and mtDNA leakage into the cytosol, which hyperactivates cGAS-STING signaling, represses SLC7A11/GPX4, and drives ferroptosis in airway epithelial cells exposed to cigarette smoke. |
Co-immunoprecipitation; chemical cross-linking; transmission electron microscopy; Rab26-/- mice; pharmacological STING inhibition; GPX4/SLC7A11 western blot |
Free radical biology & medicine |
Medium |
42176907
|
| 2026 |
Rab26 stabilizes EPOR by preventing its ubiquitin-mediated proteasomal degradation; Rab26 deficiency upregulates the E3 ligase BTRC, which interacts with EPOR to promote EPOR degradation. This reduces EPOR levels, suppresses the PPARγ/GPX4 and PINK1-mediated mitophagy axes, and sensitizes macrophages to ferroptosis. |
Co-IP of BTRC with EPOR; Rab26 KO macrophages; EPOR and BTRC protein level measurement; PPARγ antagonism; mitophagy assays; ferroptosis (lipid peroxidation, GPX4) assays; CLP sepsis mouse model |
Free radical biology & medicine |
Medium |
42086108
|