Affinage

RAB37

Ras-related protein Rab-37 · UniProt Q96AX2

Length
223 aa
Mass
24.8 kDa
Annotated
2026-06-10
31 papers in source corpus 26 papers cited in narrative 26 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RAB37 is a small Rab GTPase that operates as a master regulator of regulated exocytosis and autophagosome biogenesis, cycling between GTP- and GDP-bound states to control vesicle trafficking across secretory, immune, and metabolic cell types (PMID:25183545, PMID:29229996, PMID:38536817). First identified on secretory granules of mast cells (PMID:10722846), RAB37 was subsequently shown to localize to insulin-containing dense-core granules in β-cells, where it controls granule docking and glucose-induced secretion through a mechanism distinct from Rab3a/Rab27a effectors (PMID:23826383), and to act as a negative regulator of mast-cell degranulation within a Rab27–Munc13-4–Rab37 complex (PMID:26931073). In its GTP-bound active state, RAB37 drives nucleotide-dependent exocytosis of a broad panel of secretory cargos — including the metastasis suppressors TIMP1 and TIMP2, thrombospondin-1, and the Wnt antagonist SFRP1 — whose extracellular actions inactivate MMPs and suppress migration, angiogenesis, and cancer stemness (PMID:25183545, PMID:28151721, PMID:30158579, PMID:30131385). This secretory output is executed through SNARE machinery, with VAMP8 and Sec22b required for trafficking and membrane fusion of RAB37–TIMP1 vesicles, the latter coupling cargo release to secretory autophagy (PMID:30165196, PMID:36457117, PMID:37151129). Active RAB37 also directly binds ATG5 to recruit the ATG5–ATG12–ATG16L1 complex to the isolation membrane and facilitate LC3B lipidation, linking it mechanistically to autophagosome formation (PMID:29229996); this autophagic activity additionally promotes p62-dependent autophagic degradation of β-catenin to suppress EMT (PMID:39699800). RAB37 activity is gated by the GEF RPGR, which accelerates GDP-to-GTP exchange via its RCC1-like domain and is required for autophagy-dependent photoreceptor survival (PMID:38536817), and is switched off by PKCα phosphorylation at threonine 172, which attenuates the GTP-bound state and abrogates metastasis suppression (PMID:29312551). In macrophages and T cells, RAB37 shapes the immune microenvironment by GTP-dependent secretion of IL-6, CHI3L1, sST2, and osteopontin and by trafficking PD-1 to the cell surface (PMID:29717487, PMID:34093869, PMID:34987649, PMID:38321486, PMID:41535255), while the GDP-bound form exerts a trafficking-independent role by sequestering STAT1 in the cytosol to drive M2 macrophage polarization (PMID:39984679).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2000 Medium

    Establishing where a then-uncharacterized Rab acts: RAB37 was placed on secretory granules of mast cells, framing it as a candidate exocytic regulator.

    Evidence GFP-tagging and fluorescence microscopy in bone marrow mast cells

    PMID:10722846

    Open questions at the time
    • No effector or cargo identified
    • Functional consequence for secretion not tested
  2. 2011 Medium

    First functional and interaction link: RAB37 controls TNF-α secretion from macrophages and engages the priming factor Munc13-1, connecting it to regulated exocytosis machinery.

    Evidence Overexpression/knockdown, LC-MS/MS interactome, co-localization in RAW264.7 macrophages

    PMID:21805469

    Open questions at the time
    • Nucleotide dependence of the Munc13-1 interaction not resolved
    • Direct vs indirect binding not distinguished
  3. 2013 Medium

    Extending RAB37 to endocrine secretion and showing mechanistic independence: it docks insulin granules and supports glucose-induced secretion without using Rab3a/Rab27a effectors.

    Evidence Confocal localization, RNAi with secretion assay, pull-down in β-cell lines and human islets

    PMID:23826383

    Open questions at the time
    • The distinct effector RAB37 uses in β-cells was not identified
    • GEF/GAP regulation in β-cells unknown
  4. 2014 High

    Defining a direct cargo and disease relevance: GTP-dependent RAB37 exocytosis of TIMP1 inactivates MMP9 to suppress metastasis, establishing a tumor-suppressive secretory axis.

    Evidence Secretomics, migration/invasion assays, tail-vein metastasis models, nucleotide-binding mutants

    PMID:25183545

    Open questions at the time
    • SNARE machinery for TIMP1 release not yet defined
    • Upstream activator of RAB37 unknown at this stage
  5. 2016 High

    Revealing nucleotide-independent and inhibitory roles: RAB37 negatively regulates mast-cell degranulation within a Rab27–Munc13-4–Rab37 complex, and additionally suppresses metastasis by exocytosing thrombospondin-1.

    Evidence siRNA, dominant-active mutants, genetic epistasis, Co-IP in RBL-2H3 cells; migration/angiogenesis/in vivo metastasis assays in ESCC

    PMID:26931073 PMID:28151721

    Open questions at the time
    • Structural basis of the Rab27–Munc13-4–Rab37 complex unresolved
    • How GTP-independent and GTP-dependent modes are partitioned in different cell types unclear
  6. 2017 High

    Connecting RAB37 to autophagosome biogenesis and identifying its off-switch: GTP-RAB37 directly binds ATG5 to nucleate ATG5-12-ATG16L1 assembly and LC3B lipidation, while PKCα phosphorylation at T172 inactivates it.

    Evidence Direct binding and Co-IP, GTP/GDP mutants, isolation-membrane localization, autophagy flux; in vitro PKCα kinase assay, T172D phospho-mimetic, in vivo metastasis

    PMID:29229996 PMID:29312551

    Open questions at the time
    • Whether autophagic and secretory functions of RAB37 are mechanistically coupled not yet addressed
    • GEF activating RAB37 still unknown
  7. 2018 Medium

    Broadening the cargo repertoire and defining the fusion machinery: RAB37 secretes SFRP1, TIMP2, and sST2 via GTP-dependent exocytosis, and VAMP8 was identified as the v-SNARE required for RAB37-TIMP1 vesicle trafficking.

    Evidence Reconstitution and xenograft assays; co-localization, Co-IP, TIRF; in vivo lung-to-lung metastasis models in cancer cells

    PMID:29717487 PMID:30131385 PMID:30158579 PMID:30165196

    Open questions at the time
    • Whether a single SNARE set handles all cargos or cargo-specific SNAREs exist not resolved
    • Selectivity determinants for distinct cargos unknown
  8. 2021 High

    Defining RAB37's immune-modulatory output: GTP-dependent IL-6 secretion drives M2 polarization and STAT3-dependent PD-1 expression in CD8+ T cells, while in stem cells RAB37 directly binds TIMP1 to drive CD63/integrin-β1/FAK adipogenic signaling.

    Evidence Vesicle isolation, imaging, ChIP, Rab37 KO syngeneic allografts; proximity ligation assay and knockdowns in hADSCs

    PMID:34093869 PMID:34858503

    Open questions at the time
    • How RAB37 cargo selection skews toward immunosuppressive secretion not resolved
    • Direct vs vesicular contributions to immune phenotypes not fully separated
  9. 2022 High

    Formalizing secretory autophagy as the trafficking route: RAB37 and Sec22b are present in autophagosomes and required, with ATG5/ATG7, for TIMP1 exocytosis; RAB37 also traffics CHI3L1 to activate AKT/β-catenin/NF-κB.

    Evidence Autophagosome purification with mass spec, ATG5/ATG7/Sec22b knockdown, in vivo metastasis; vesicle isolation, TIRF, Rab37 KO splenocytes/BMDMs

    PMID:34987649 PMID:36457117

    Open questions at the time
    • Trigger that diverts cargo into secretory vs degradative autophagy not defined
    • Stoichiometry of RAB37-Sec22b on the autophagosome unknown
  10. 2023 Medium

    Linking stimulus to dual output: starvation-activated GTP-RAB37 simultaneously increases LC3-II and drives Sec22b-dependent TIMP1 secretion, unifying autophagy activation and secretion; RAB37 also directly binds Hsp90α and TIMP1 to support angiogenic ADSC functions.

    Evidence Overexpression/knockdown, LC3-II immunoblotting, Sec22b siRNA, lung-to-lung metastasis; proximity ligation assay and LC-MS/MS of conditioned media in ADSCs, db/db wound model

    PMID:36627432 PMID:37151129

    Open questions at the time
    • Mechanism coupling starvation sensing to RAB37 activation not defined
    • Whether Hsp90α and TIMP1 share the same vesicle population unresolved
  11. 2024 High

    Completing the regulatory cycle and revealing a trafficking-independent function: RPGR was identified as the GEF activating RAB37 to support retinal autophagy, while GDP-bound RAB37 sequesters STAT1 in the cytosol to promote M2 polarization; RAB37 also traffics PD-1, degrades β-catenin via p62, and is transcriptionally driven by E2F1/EGR2 for autophagy in oocytes.

    Evidence In vitro GEF kinetics, Co-IP, Rpgr KO mouse with AAV rescue; GDP-mutant Co-IP and fractionation in BMDMs; PD-1 glycosylation-mutant imaging and Rab37 KO tumors; p62-β-catenin Co-IP with chloroquine rescue; conditional oocyte KO with ChIP

    PMID:38321486 PMID:38536817 PMID:39113565 PMID:39699800 PMID:39984679

    Open questions at the time
    • GAP that terminates RAB37 GTP signaling not identified
    • How the same protein partitions between exocytic, autophagic, and STAT1-sequestering roles in a given cell not resolved
  12. 2025 Medium

    Integrating RAB37 into a tumor-microenvironment feedback circuit: macrophage RAB37 promotes osteopontin secretion that sustains an autocrine STAT3/Spp1 loop enforcing M2 polarization and a Spp1+ immunosuppressive TAM state.

    Evidence Single-cell RNA sequencing, Rab37 KO tumor model, OPN secretion assay, paracrine co-culture

    PMID:41535255

    Open questions at the time
    • Nucleotide-state requirement for OPN secretion vs STAT1 sequestration not disentangled
    • Therapeutic tractability of the OPN loop untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a single Rab GTPase selects among its many cargos and partitions between GTP-dependent exocytosis, autophagosome biogenesis, and GDP-state STAT1 sequestration within one cell remains unresolved, as does the identity of its GAP.
  • No GAP identified for RAB37
  • No structural model of cargo-selective recognition
  • Spatial/temporal control distinguishing degradative vs secretory autophagy unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003924 GTPase activity 6 GO:0060090 molecular adaptor activity 2 GO:0140313 molecular sequestering activity 1
Localization
GO:0031410 cytoplasmic vesicle 4 GO:0005829 cytosol 1
Pathway
R-HSA-168256 Immune System 5 R-HSA-5653656 Vesicle-mediated transport 4 R-HSA-9612973 Autophagy 4
Complex memberships
ATG5-ATG12-ATG16L1 complexRab27-Munc13-4-Rab37 complex

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 Rab37 is a novel Rab GTPase specifically expressed in mast cells (MC-9 line and bone marrow mast cells) and localizes to secretory granules, as shown by GFP-tagged Rab37 expression in bone marrow mast cells. GFP-tagging and fluorescence microscopy in bone marrow mast cells FEBS letters Medium 10722846
2011 Rab37 controls TNF-α secretion from activated macrophages; overexpression of wild-type or constitutively active Rab37 increases TNF-α secretion while siRNA knockdown decreases it. Rab37 interacts with Munc13-1, and TNF-α-containing vesicles co-localize with both Rab37 and Munc13-1. Overexpression/knockdown (siRNA), LC-MS/MS interactome, immunocytochemistry co-localization in RAW264.7 macrophages European journal of immunology Medium 21805469
2011 Rab37 is identified as a MetAP-2-specific substrate; aberrant accumulation of Rab37 (when N-terminal methionine excision is blocked by MetAP-2 inhibitor TNP-470) disrupts Wnt planar cell polarity (PCP) signaling. A Rab37 point mutant resistant to NME phenocopies MetAP-2 inhibition on Wnt PCP-dependent processes. MetAP-2 inhibitor treatment, NME-resistant Rab37 point mutant expression, functional PCP signaling assays Chemistry & biology Medium 22035799
2013 Rab37 localizes to insulin-containing large dense core granules in pancreatic β-cells, and its knockdown by RNAi impairs glucose-induced insulin secretion and reduces granule docking at the plasma membrane. Pull-down experiments show Rab37 does not interact with known Rab3a or Rab27a effectors, indicating it operates through a distinct mechanism. Confocal microscopy localization, RNAi knockdown with secretion assay, pull-down experiments in β-cell lines and human islets PloS one Medium 23826383
2014 RAB37 directly targets TIMP1 as a secretory cargo and regulates TIMP1 exocytosis in a nucleotide-dependent (GTP-dependent) manner; secreted TIMP1 inactivates MMP9 to suppress cancer cell migration in vitro and in vivo. Dysfunction of RAB37 abrogates metastasis suppression. Secretomics, cell migration/invasion assays, animal (tail-vein injection) metastasis models, nucleotide-binding mutant analysis Nature communications High 25183545
2016 In mast cells, Rab37 acts as a negative regulator of degranulation by interacting with Munc13-4 in a GTP-independent manner, forming a Rab27-Munc13-4-Rab37 complex that counteracts the vesicle-priming activity of the Rab27-Munc13-4 system. Knockdown of Rab37 or overexpression of dominant-active Rab37 both enhance degranulation; the hypersecretion phenotype in Rab37-knockdown cells is suppressed by simultaneous knockdown of Rab27a/b or Munc13-4. siRNA knockdown, dominant-active mutant overexpression, genetic epistasis (double knockdown), immunoprecipitation in RBL-2H3 mast cells Scientific reports High 26931073
2016 Rab37-mediated exocytosis of thrombospondin-1 (TSP1) from cancer cells inhibits angiogenesis and suppresses metastasis; secreted TSP1 inhibits p-FAK/p-paxillin/p-ERK migration signaling in both cancer epithelial cells and surrounding endothelial cells. Dysfunction of Rab37 or loss of TSP1 abolishes these suppressive effects. Cell migration/invasion, angiogenesis, and in vivo metastasis assays; conditioned medium experiments; signaling pathway analysis in ESCC cells Clinical cancer research Medium 28151721
2017 RAB37 directly binds ATG5 and promotes autophagosome formation by recruiting ATG5-12 to the isolation membrane and facilitating assembly of the ATG5-ATG12-ATG16L1 complex. GTP-bound RAB37 shows enhanced interaction with ATG5-12, while GDP-stabilized mutation impairs the interaction. RAB37 promotes ATG5-12 interaction with ATG16L1, facilitating LC3B lipidation in a GTP-dependent manner. Direct binding assay, mutation analysis (GTP/GDP-binding mutants), Co-IP, isolation membrane localization, autophagy flux assays, knockdown and overexpression Cell death and differentiation High 29229996
2017 PKCα phosphorylates Rab37 at threonine 172 (T172), leading to attenuation of its GTP-bound state, impairment of Rab37-mediated TIMP1 exocytosis, and reduction of metastasis suppression. Phospho-mimetic T172D mutant of Rab37 promotes tumor metastasis in vivo. PKCα reduces vesicle co-localization of Rab37 and TIMP1. In vitro kinase assay (PKCα phosphorylation of Rab37), site-directed mutagenesis (T172D phospho-mimetic), vesicle co-localization by confocal microscopy, in vivo metastasis assay Oncotarget High 29312551
2018 Rab37 mediates exocytosis of secreted frizzled-related protein-1 (SFRP1), an extracellular Wnt antagonist, to suppress Wnt signaling and cancer stemness in vitro and in vivo. Reconstitution experiments show SFRP1 secretion is crucial for Rab37-mediated cancer stemness suppression. Reconstitution experiments, SFRP1 recombinant protein treatment, xenograft tumor initiation assay, signaling pathway analysis Cell death & disease Medium 30158579
2018 VAMP8 (a v-SNARE) interacts with RAB37 and is required for TIMP1 exocytosis. VAMP8 co-localizes with RAB37 and facilitates trafficking of RAB37-TIMP1 vesicles. Reconstitution experiments (tail-vein injection, lung-to-lung metastasis) demonstrate VAMP8 is essential for RAB37-regulated vesicle trafficking of TIMP1 to suppress cancer metastasis. Confocal and TIRF microscopy, Co-IP, in vivo reconstitution assays (tail-vein injection, lung-to-lung metastasis mouse model) Cancer letters Medium 30165196
2018 Rab37 mediates secretion of soluble ST2 (sST2) from lung cancer cells in a GTP-dependent manner, and secreted sST2 skews macrophage polarization toward anti-tumoral M1-like phenotype both in vitro and in xenografts. Overexpression/knockdown system, GTP/GDP mutant analysis, macrophage polarization assays, xenograft tumor model International journal of cancer Medium 29717487
2018 RAB37 co-localizes with TIMP2 and regulates TIMP2 secretion in nasopharyngeal carcinoma cells, thereby inhibiting MMP2 activity and suppressing cell metastasis. RAB37 downregulation is attributed to hypermethylation of its promoter. Co-localization assay, secretion assay, MMP2 activity assay, ectopic overexpression and in vivo validation Clinical cancer research Medium 30131385
2020 RAB37 phosphorylation by PKCα (via the miR-200b/PKCα axis) is promoted by methionine treatment in gastric cancer stem cells, inactivating RAB37 and suppressing RAB37-mediated autophagy. Methionine also enhances RAB37 methylation. Methionine lyase (Metase) treatment reduces RAB37 phosphorylation and methylation, restoring autophagy. Lentiviral expression of methionine lyase, miR-200b/PKCα pathway analysis, methylation and phosphorylation assays, autophagy measurement in GCSCs Cell cycle Medium 32926650
2021 Rab37 in macrophages regulates IL-6 secretion in a GTPase-dependent manner, promoting M2 macrophage polarization. Macrophage-derived IL-6 promotes STAT3-dependent PD-1 mRNA expression in CD8+ T cells. These mechanisms were demonstrated using vesicle isolation, imaging, and chromatin immunoprecipitation showing STAT3 binding to the PD-1 promoter. Vesicle isolation, imaging analyses, ChIP assay for STAT3 binding at PD-1 promoter, Rab37 knockout mice syngeneic allograft, GTP/GDP mutant analysis Theranostics High 34093869
2021 RAB37 promotes adipogenic differentiation of hADSCs via TIMP1 secretion; RAB37 directly interacts with TIMP1 (shown by proximity ligation assay), and secreted TIMP1 signals through CD63/integrin β1 to promote FAK phosphorylation (Tyr397). Knockdown of TIMP1, CD63, or FAK inhibition impedes RAB37-mediated adipogenesis. Proximity ligation assay (direct interaction), cytokine array, ELISA, knockdown experiments, FAK phosphorylation assays in hADSCs Stem cells international Medium 34858503
2022 Rab37 mediates CHI3L1 (chitinase 3-like-1) intracellular vesicle trafficking and exocytosis in T cells and macrophages in a GTP-dependent manner; this is abolished in Rab37 knockout mice splenocytes and BMDMs, and attenuated with inactive GDP-bound Rab37. Secreted CHI3L1 activates AKT, β-catenin, and NF-κB signaling in cancer cells and macrophages. Vesicle isolation, TIRF microscopy, real-time confocal microscopy, Rab37 knockout mouse splenocytes/BMDMs, GTP/GDP mutant analysis Theranostics High 34987649
2022 Secretory autophagy promotes RAB37-mediated TIMP1 exocytosis in a RAB37- and Sec22b-dependent manner. Knockdown of Atg5 or Atg7 in cells harboring active RAB37 decreases autophagy and TIMP1 secretion. RAB37 and Sec22b proteins were identified in purified autophagosomes. Sec22b (a SNARE) participates in vesicle/membrane fusion of secretory autophagy. Autophagosome purification (mass spec identification of RAB37 and Sec22b), immunoblotting, TEM, immunofluorescence, siRNA knockdown of ATG5/ATG7/Sec22b, lung-to-lung metastasis mouse model Journal of biomedical science High 36457117
2023 Starvation-activated RAB37 simultaneously drives autophagy activation and TIMP1 secretion via secretory autophagy in a Sec22b-dependent manner. Active GTP-bound RAB37 increases LC3-II levels and TIMP1 secretion; knockdown of Sec22b decreases TIMP1 secretion without affecting proliferation. Overexpression/knockdown system, LC3-II immunoblotting, motility assays, lung-to-lung mouse metastasis model, Sec22b siRNA Autophagy Medium 37151129
2023 Rab37 directly binds Hsp90α and TIMP1 in ADSCs (shown by proximity ligation assay), regulates their secretion, and promotes ADSC proliferation, migration, and endothelial differentiation. Knockdown of Hsp90α or TIMP1 compromises Rab37's promoting effects. Proximity ligation assay, LC-MS/MS of conditioned media, ELISA, knockdown experiments, in vivo diabetic wound healing model (db/db mice) Stem cell reviews and reports Medium 36627432
2024 RPGR (retinitis pigmentosa GTPase regulator) is a guanine nucleotide exchange factor (GEF) for RAB37 that activates it by accelerating GDP-to-GTP exchange. RPGR directly interacts with RAB37 via the RPGR-RCC1-like domain. Rpgr knockout in mice leads to photoreceptor degeneration due to autophagy impairment; this is rescued by AAV-mediated restoration of RPGR, which re-activates RAB37-mediated autophagy. GEF activity assay (GDP-to-GTP exchange kinetics), Co-IP/direct interaction assay, Rpgr knockout mouse, AAV-mediated gene rescue, autophagy flux measurement in retina Cell reports High 38536817
2024 Rab37 mediates intracellular trafficking and plasma membrane presentation of PD-1 in T cells in a GTP-dependent manner. PD-1 co-localizes with Rab37-specific vesicles, and glycosylation-deficient PD-1 mutant shows delayed cargo recruitment to Rab37 vesicles and stalled membrane presentation. Tumor-infiltrating T cells from Rab37 knockout mice show upregulated proliferation and activity. Confocal imaging, biochemical co-localization, glycosylation mutant PD-1 analysis, Rab37 knockout mouse tumor model, GTP/GDP mutant analysis Journal of biomedical science Medium 38321486
2024 Conditional knockout of Rab37 in oocytes impairs autophagy in the ovary and interferes with follicular homeostasis and ovary development in mice. E2F1 and EGR2 transcription factors synergistically activate Rab37 transcription and promote autophagy. Conditional knockout mouse model, autophagy flux assays, ChIP/promoter analysis for E2F1 and EGR2, flunarizine rescue experiment Autophagy Medium 39113565
2024 GDP-bound Rab37 (inactive form) interacts with the nuclear localization sequence of STAT1 to sequester it in the cytosol, preventing STAT1 nuclear translocation and transcriptional activation of type I IFN pathway genes, thereby promoting M2-like macrophage polarization. This represents a vesicle trafficking-independent function of Rab37. cDNA microarray (Rab37 KO vs WT BMDMs), Co-IP of GDP-Rab37 with STAT1, subcellular fractionation showing STAT1 cytosolic retention, in vitro/in vivo assays British journal of cancer Medium 39984679
2024 RAB37 promotes autophagic degradation of β-catenin in gastric cancer cells by strengthening the interaction between p62 and β-catenin; this requires RAB37 GTPase activity. The effect on EMT suppression, migration, and invasion is reversed by the autophagy inhibitor chloroquine. Co-IP (p62-β-catenin interaction), GTPase-dead mutant, autophagy inhibitor (chloroquine) rescue, Western blot for autophagy markers, in vivo pulmonary metastasis mouse model Cellular oncology Medium 39699800
2025 Rab37 promotes osteopontin (OPN) secretion in macrophages, which activates STAT3 signaling to establish an autocrine feedback loop sustaining Spp1 expression and inducing M2-like polarization. Paracrine OPN signaling enhances lung cancer cell proliferation, migration, and invasion. Rab37 KO tumors showed higher proportion of Thbs1+ TAMs versus immunosuppressive Spp1+ TAMs in WT tumors. Single-cell RNA sequencing, Rab37 KO mouse tumor model, OPN secretion assay, STAT3 pathway analysis, paracrine co-culture experiments Oncogenesis Medium 41535255

Source papers

Stage 0 corpus · 31 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 RAB37 interacts directly with ATG5 and promotes autophagosome formation via regulating ATG5-12-16 complex assembly. Cell death and differentiation 81 29229996
2021 Converged Rab37/IL-6 trafficking and STAT3/PD-1 transcription axes elicit an immunosuppressive lung tumor microenvironment. Theranostics 67 34093869
2000 Rab37 is a novel mast cell specific GTPase localized to secretory granules. FEBS letters 65 10722846
2014 Small GTPase Rab37 targets tissue inhibitor of metalloproteinase 1 for exocytosis and thus suppresses tumour metastasis. Nature communications 53 25183545
2016 Dysregulation of Rab37-Mediated Cross-talk between Cancer Cells and Endothelial Cells via Thrombospondin-1 Promotes Tumor Neovasculature and Metastasis. Clinical cancer research : an official journal of the American Association for Cancer Research 48 28151721
2011 Release of TNF-α from macrophages is mediated by small GTPase Rab37. European journal of immunology 46 21805469
2022 Targeting protumor factor chitinase-3-like-1 secreted by Rab37 vesicles for cancer immunotherapy. Theranostics 43 34987649
2013 The GTPase Rab37 Participates in the Control of Insulin Exocytosis. PloS one 33 23826383
2018 Rab37 mediates exocytosis of secreted frizzled-related protein 1 to inhibit Wnt signaling and thus suppress lung cancer stemness. Cell death & disease 31 30158579
2018 Rab37 in lung cancer mediates exocytosis of soluble ST2 and thus skews macrophages toward tumor-suppressing phenotype. International journal of cancer 30 29717487
2018 RAB37 Hypermethylation Regulates Metastasis and Resistance to Docetaxel-Based Induction Chemotherapy in Nasopharyngeal Carcinoma. Clinical cancer research : an official journal of the American Association for Cancer Research 28 30131385
2016 Mast cell degranulation is negatively regulated by the Munc13-4-binding small-guanosine triphosphatase Rab37. Scientific reports 25 26931073
2011 Disruption of Wnt planar cell polarity signaling by aberrant accumulation of the MetAP-2 substrate Rab37. Chemistry & biology 24 22035799
2018 The small GTPase RAB37 functions as an organizer for autophagosome biogenesis. Autophagy 23 29388490
2022 Secretory autophagy promotes Rab37-mediated exocytosis of tissue inhibitor of metalloproteinase 1. Journal of biomedical science 22 36457117
2018 VAMP8, a vesicle-SNARE required for RAB37-mediated exocytosis, possesses a tumor metastasis suppressor function. Cancer letters 22 30165196
2024 IL-33/NF-κB/ST2L/Rab37 positive-feedback loop promotes M2 macrophage to limit chemotherapeutic efficacy in lung cancer. Cell death & disease 18 38778059
2020 Methionine represses the autophagy of gastric cancer stem cells via promoting the methylation and phosphorylation of RAB37. Cell cycle (Georgetown, Tex.) 17 32926650
2017 Phosphorylation of Rab37 by protein kinase C alpha inhibits the exocytosis function and metastasis suppression activity of Rab37. Oncotarget 13 29312551
2024 Rab37 mediates trafficking and membrane presentation of PD-1 to sustain T cell exhaustion in lung cancer. Journal of biomedical science 10 38321486
2024 RPGR is a guanine nucleotide exchange factor for the small GTPase RAB37 required for retinal function via autophagy regulation. Cell reports 9 38536817
2024 RAB37-mediated autophagy guards ovarian homeostasis and function. Autophagy 9 39113565
2023 Secretory autophagy-promoted cargo exocytosis requires active RAB37. Autophagy 9 37151129
2022 Knockout of GGPPS1 restrains rab37-mediated autophagy in response to ventilator-induced lung injury. Human cell 8 35334098
2013 An association study on genetic polymorphisms of Rab37 gene with the risk of esophageal squamous cell carcinoma in a Chinese Han population. International journal of medical sciences 6 23372429
2023 Rab37 Promotes Endothelial Differentiation and Accelerates ADSC-Mediated Diabetic Wound Healing through Regulating Secretion of Hsp90α and TIMP1. Stem cell reviews and reports 5 36627432
2021 RAB37 Promotes Adipogenic Differentiation of hADSCs via the TIMP1/CD63/Integrin Signaling Pathway. Stem cells international 5 34858503
2020 RAB37 multiple alleles, transcription activation and evolution in mammals. International journal of biological sciences 5 33061809
2026 Rab37-mediated OPN secretion enriches SPP1+ macrophages through autocrine-paracrine signaling to drive lung tumor progression. Oncogenesis 1 41535255
2025 GDP-bound Rab37 modulates M2-like tumor-associated macrophage polarization by attenuating STAT1 translocation to downregulate the type I IFN pathway. British journal of cancer 1 39984679
2024 RAB37 suppresses the EMT, migration and invasion of gastric cancer cells by mediating autophagic degradation of β-catenin. Cellular oncology (Dordrecht, Netherlands) 0 39699800

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