Affinage

SNX5

Sorting nexin-5 · UniProt Q9Y5X3

Length
404 aa
Mass
46.8 kDa
Annotated
2026-04-28
26 papers in source corpus 22 papers cited in narrative 22 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SNX5 is a PX-BAR domain sorting nexin that functions as a central regulator of endosomal membrane trafficking, controlling retrograde transport, cargo recycling, macropinocytosis, and receptor fate decisions across diverse cell types. As a component of the ESCPE-1 retromer-associated coat, SNX5 heterodimerizes with SNX1 or SNX6 on early endosomes and mediates endosome-to-TGN retrieval of cargoes including CI-MPR, VMAT, and EGFR; its PX domain binds PtdIns(3)P and PtdIns(3,4)P₂ for membrane recruitment, while the BAR domain drives membrane tubulation and also serves as a docking site for the MuRF2/MuRF3 E3 ubiquitin ligases that regulate SNX5 turnover (PMID:17148574, PMID:35426896, PMID:18854019, PMID:41077709). Beyond retrograde sorting, SNX5 promotes macropinosome biogenesis in macrophages independently of SNX1, facilitates plasma membrane recycling of receptors such as EGFR and LRP5/6 to sustain downstream signaling (EGF, Wnt, PKA pathways), and recruits CHC22 clathrin to ERGIC membranes for GLUT4 Golgi-bypass trafficking (PMID:23213485, PMID:41714616, PMID:39922976, PMID:39160272). SNX5 additionally stabilizes PKA regulatory subunit RIα on early endosomes, linking endosomal sorting to PKA signaling, HDAC5 stability, and myogenic differentiation; its own stability is controlled by MuRF2-mediated K48-ubiquitination and USP46-mediated deubiquitination (PMID:41077709, PMID:39909216).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1999 Medium

    The initial molecular characterization of SNX5 established it as a PX-domain protein capable of physically engaging the Fanconi anemia protein FANCA, hinting at roles beyond simple phosphoinositide binding.

    Evidence Yeast two-hybrid screen and co-immunoprecipitation with FANCA deletion mapping in human cells

    PMID:10600472

    Open questions at the time
    • Functional consequence of SNX5–FANCA interaction on Fanconi anemia pathway is undefined
    • FANCA binding domain in SNX5 was not precisely mapped beyond exclusion of PX domain
    • No in vivo validation
  2. 2006 High

    Placing SNX5 in the retromer pathway resolved whether additional SNX-BAR proteins beyond SNX1/SNX2 are required for endosome-to-TGN cargo retrieval, establishing SNX5 and SNX6 as essential components whose loss phenocopies retromer disruption and destabilizes SNX1.

    Evidence RNAi knockdown of SNX5/SNX6 in HeLa cells with CI-MPR redistribution phenotype; co-IP and colocalization with SNX1

    PMID:17148574

    Open questions at the time
    • Direct cargo-binding mechanism of SNX5 was not determined
    • Whether SNX5 and SNX6 are functionally redundant was not resolved
  3. 2006 Medium

    Discovery of SNX5 interaction with Mind bomb (Mib) in zebrafish linked endosomal sorting to Notch ligand endocytosis, expanding SNX5 function beyond retromer-mediated recycling to developmental signaling.

    Evidence Yeast two-hybrid and colocalization in zebrafish; morpholino knockdown causing hematopoietic and vascular defects

    PMID:16857196 PMID:25645681

    Open questions at the time
    • Direct biochemical reconstitution of SNX5–Mib–Delta sorting not performed
    • Mammalian conservation of this interaction not demonstrated
  4. 2008 High

    Two parallel studies revealed that SNX5 operates not only in retrograde transport but also at the plasma membrane: its PX domain binds PtdIns(3,4)P₂ to drive macropinocytosis downstream of EGFR, while its endosomal interaction with DOCK180 (via DHR1) is required for CI-MPR retrieval independently of Rac1 GEF activity.

    Evidence PX domain lipid-binding assays and EGF-stimulated macropinosome quantification; nanoflow LC-MS/MS DOCK180 interactome with co-IP and CI-MPR rescue by DHR1 domain expression

    PMID:18596235 PMID:18854019

    Open questions at the time
    • How SNX5 coordinates its dual plasma membrane and endosomal functions spatiotemporally is unclear
    • DOCK180 scaffolding mechanism on endosomes not structurally resolved
  5. 2012 High

    Demonstrating that SNX5 is essential for macropinosome biogenesis in primary macrophages independently of SNX1 resolved whether SNX5's macropinocytosis role is merely secondary to its retromer function, establishing a distinct trafficking arm.

    Evidence siRNA depletion in bone marrow-derived macrophages; SNX1 KO mice showed no macropinocytosis defect

    PMID:23213485

    Open questions at the time
    • Mechanism by which SNX5 promotes actin-dependent membrane ruffling not defined
    • Whether SNX5 cooperates with SNX6 or other BAR proteins in macropinocytosis not tested
  6. 2017 High

    The finding that SNX5 stabilizes insulin-degrading enzyme (IDE) at the proximal tubule brush border and regulates renal insulin metabolism extended SNX5 function to metabolic physiology in vivo.

    Evidence Co-IP and colocalization of SNX5–IDE in human renal cells; siRNA silencing in mice decreased IDE levels and urinary insulin excretion

    PMID:29080975

    Open questions at the time
    • Direct versus indirect mechanism of IDE stabilization by SNX5 not distinguished
    • Whether this reflects canonical retrograde transport of IDE is unknown
  7. 2019 Medium

    Identification of SNX5 as a negative regulator of RIG-I signaling via promotion of K48 ubiquitination of RIG-I revealed a previously unknown immunoregulatory function.

    Evidence Overexpression/knockdown with luciferase reporters and ubiquitination assays in HEK293T cells

    PMID:31806368

    Open questions at the time
    • The E3 ligase mediating SNX5-dependent K48 ubiquitination of RIG-I was not identified
    • Mechanism not reconstituted in vitro
    • In vivo antiviral relevance not tested
  8. 2022 High

    Establishing SNX5 as required for VMAT retrograde transport to the TGN and subsequent AP-3-dependent dense core vesicle loading connected endosomal sorting to regulated monoamine secretion.

    Evidence SNX5 knockout with VMAT trafficking and monoamine release assays; genetic interaction with AP-3

    PMID:35426896

    Open questions at the time
    • Whether SNX5 directly recognizes a sorting motif in VMAT is unresolved
    • Neuronal in vivo consequences of SNX5 loss on monoamine signaling not assessed
  9. 2023 Medium

    Discovery that SNX5 recruits VPS13A to endosomes via a PxP–VAB domain interaction linked SNX5 to lipid transfer at membrane contact sites and to VPS13-associated neurodegeneration.

    Evidence Co-IP with VAB domain mutagenesis (pathogenic asparagine mutation); colocalization of VPS13A fragments with SNX5

    PMID:36977596

    Open questions at the time
    • Functional consequence of VPS13A–SNX5 interaction for lipid transfer not demonstrated
    • Whether this interaction is required for VPS13A disease pathogenesis is untested
  10. 2024 High

    Three studies in 2024 diversified SNX5 cargo repertoire and cell-type contexts: SNX5 recruits CHC22 clathrin to ERGIC for GLUT4 Golgi-bypass trafficking, promotes lysosome-to-synapse recruitment for B cell antigen extraction, and binds Rab11a to sustain LRP6 surface expression and protect against cardiac hypertrophy.

    Evidence Co-IP/domain mapping and GLUT4 trafficking assays (CHC22); live imaging of B cell immune synapses with SNX5 knockdown; co-IP and AAV9-cardiac overexpression of SNX5 with echocardiography

    PMID:38950816 PMID:39160272 PMID:39448266

    Open questions at the time
    • Whether CHC22 recruitment and ESCPE-1 function are mutually exclusive or coordinated is unresolved
    • Structural basis of SNX5–Rab11a interaction not defined
    • B cell phenotype awaits in vivo immune challenge confirmation
  11. 2025 Medium

    Multiple 2025 studies uncovered SNX5 regulation by ubiquitin signaling (MuRF2 ubiquitination, USP46 deubiquitination), its role in stabilizing PKA-RIα on endosomes to control myogenic differentiation, its trafficking of EGFR and LRP5 to sustain receptor signaling, and its involvement in α-synuclein toxicity via TGN integrity.

    Evidence SILAC AP-MS, CRISPR KO, ubiquitination-site mapping for MuRF2/MuRF3–SNX5 axis; USP46 interactome and epistasis; Snx5-deficient EGFR trafficking assay; co-IP of SNX5–LRP5 with Wnt readout; genome-wide siRNA screen for α-synuclein toxicity in human neurons

    PMID:39909216 PMID:39922976 PMID:40457499 PMID:41077709 PMID:41714616

    Open questions at the time
    • Structural basis of MuRF2–BAR domain interaction not resolved
    • Whether SNX5-dependent ferroptosis is a general phenomenon or specific to ischemia-reperfusion injury is unclear
    • In vivo neurodegenerative consequences of SNX5 manipulation in α-synuclein models not yet tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the structural basis for SNX5 cargo selectivity versus SNX6 across the expanding cargo repertoire, how SNX5's multiple interactors are spatiotemporally coordinated on distinct endosomal subdomains, and whether SNX5 loss causes a coherent disease phenotype in mammals.
  • No complete structural model of SNX5 in complex with physiological cargo on membranes
  • Functional redundancy between SNX5 and SNX6 across tissue types not systematically addressed
  • No Mendelian disease directly attributed to SNX5 mutations in humans

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 2 GO:0008289 lipid binding 1
Localization
GO:0005768 endosome 5 GO:0005886 plasma membrane 3 GO:0005794 Golgi apparatus 2 GO:0031410 cytoplasmic vesicle 2 GO:0005829 cytosol 1
Pathway
R-HSA-9609507 Protein localization 5 R-HSA-5653656 Vesicle-mediated transport 4 R-HSA-162582 Signal Transduction 3 R-HSA-168256 Immune System 3 R-HSA-392499 Metabolism of proteins 3
Partners
CHC22DOCK180MURF2RAB11ASNX1SNX6USP46VPS13A
Complex memberships
ESCPE-1 (SNX-BAR retromer coat)SNX1-SNX5 heterodimerSNX5-SNX6 heterodimer

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2006 SNX5 and SNX6 were identified as functional components required for retromer-mediated endosome-to-trans-Golgi-network retrieval of the cation-independent mannose-6-phosphate receptor (CI-MPR). RNAi knockdown of SNX5 or SNX6 phenocopied suppression of known retromer components, and SNX5 colocalized with SNX1 on early endosomes. Suppression of SNX5 and/or SNX6 caused significant post-translational loss of SNX1. RNAi loss-of-function screen, immunoprecipitation, colocalization by fluorescence microscopy Journal of cell science High 17148574
1999 SNX5 was identified as a binding partner of the Fanconi anemia complementation group A (FANCA) protein via yeast two-hybrid screening, confirmed by immunoprecipitation. Deletion mutant analysis showed the PX domain of SNX5 is not required for FANCA binding. Overexpression of SNX5 increased FANCA protein levels. Yeast two-hybrid screening, immunoprecipitation, deletion mutant analysis, overexpression Biochemical and biophysical research communications Medium 10600472
2008 SNX5 promotes macropinocytosis through its PX domain, which specifically interacts with PtdIns(3)P and PtdIns(3,4)P2. SNX5 is recruited to plasma membrane regions containing EGF receptor or PtdIns(3,4)P2, and this recruitment requires EGFR tyrosine kinase activity. Overexpression of SNX5 approximately doubled macropinosome formation; inhibition of EGFR kinase prevented SNX5 plasma membrane recruitment and macropinosome formation. Stable GFP-SNX5 expression, PX domain lipid-binding assays, EGF stimulation, EGFR kinase inhibitor (AG1478), fluorescence microscopy BMC cell biology Medium 18854019
2012 SNX5 is essential for macropinosome biogenesis in primary mouse macrophages independently of SNX1. Depletion of SNX5 in bone marrow-derived macrophages dramatically decreased number and size of macropinosomes and reduced uptake and processing of soluble ovalbumin, demonstrating SNX5's role in antigen delivery to late endosomes. SNX1 knockout had no effect on SNX5 localization or macropinosome biogenesis. siRNA depletion, SNX1 knockout mouse macrophages, fluorescence microscopy, ovalbumin uptake assay Biology open High 23213485
2006 Zebrafish Snx5 (ortholog) was identified as a direct binding partner of Mind bomb (Mib), an E3 ubiquitin ligase required for Notch signaling, via yeast two-hybrid screening. Snx5 colocalizes with Mib in early endosomal compartments. Morpholino knockdown of snx5 in zebrafish caused defects in hematopoiesis and blood vessel development. Yeast two-hybrid, colocalization by fluorescence microscopy, morpholino knockdown in zebrafish FEBS letters Medium 16857196
2015 In zebrafish, SNX5 (ortholog) directly binds to Mind bomb (Mib) and co-localizes with Mib and Delta complexes. SNX5 functions as a vital partner of Mib in promoting endocytosis of Delta and subsequent Notch signaling activation. miR-216a regulates snx5 expression to modulate Notch pathway activity during retinal development. Co-localization, morpholino knockdown, overexpression, miRNA gain/loss-of-function in zebrafish Developmental biology Medium 25645681
2008 The DHR1 domain of DOCK180 binds to SNX5 (and SNX1, SNX2, SNX6) as identified by nanoflow LC-MS/MS. Among the SNX proteins, SNX5 was coimmunoprecipitated with DOCK180 most efficiently. DOCK180 colocalized with SNX5 at endosomes. RNAi knockdown of either SNX5 or DOCK180 caused redistribution of CI-MPR from TGN to endosomes. Expression of the DHR1 domain alone was sufficient to restore CI-MPR distribution in DOCK180 knockdown cells, and this function was independent of DOCK180's GEF activity toward Rac1. Nanoflow LC-MS/MS interactome, co-immunoprecipitation, RNAi knockdown, CI-MPR localization assay, fluorescence microscopy Molecular biology of the cell High 18596235
2017 SNX5 co-localizes with and co-immunoprecipitates with the insulin-degrading enzyme (IDE) at the plasma membrane and perinuclear area of human renal proximal tubule cells and in the brush border membrane of proximal tubules. Insulin increases co-localization and co-immunoprecipitation of SNX5 and IDE. Silencing SNX5 in cells decreased IDE expression and activity; renal-selective silencing in mice decreased IDE protein levels and urinary insulin excretion, impairing insulin and glucose responses. Co-immunoprecipitation, colocalization by fluorescence microscopy, siRNA silencing in vitro and in vivo, IDE activity assay, mouse metabolic phenotyping Diabetologia High 29080975
2019 SNX5 negatively regulates RIG-I-like receptor (RLR)-mediated antiviral signaling. Overexpression of SNX5 inhibits virus-induced activation of the IFN-β promoter, ISRE, NF-κB, and IRF3. SNX5 promotes K48 ubiquitination and attenuates K63 ubiquitination of RIG-I, leading to decreased RIG-I expression. SNX5 overexpression also weakens the interaction between VISA and TRAF2/5. Overexpression, RNAi knockdown, luciferase reporter assays, ubiquitination assays, co-immunoprecipitation Biochemical and biophysical research communications Medium 31806368
2022 SNX5 is required for retrograde transport of the vesicular monoamine transporter (VMAT) from endosomes to the TGN. Loss of SNX5 disrupts VMAT trafficking to dense core vesicles (DCVs) and impairs regulated monoamine release. SNX5-mediated retrograde transport enables AP-3 to assemble DCV cargo at the TGN, revealing a transient role for AP-3 at the TGN. Loss-of-function (SNX5 knockout), VMAT trafficking assays, monoamine release assays, fluorescence microscopy The Journal of cell biology High 35426896
2023 SNX5 interacts with VPS13A via the VPS13 adaptor-binding (VAB) domain in VPS13A and a PxP motif in SNX5, mediating VPS13A association with endosomal subdomains. Mutation of a conserved asparagine residue in the VAB domain (also pathogenic in VPS13D) impairs this interaction. VPS13A fragments containing the VAB domain co-localize with SNX5. Co-immunoprecipitation, colocalization by fluorescence microscopy, mutagenesis of VAB domain, domain mapping of PxP motif in SNX5 Life science alliance Medium 36977596
2024 SNX5 interacts with the C-terminal trimerization domain of CHC22 clathrin (but not CHC17), and SNX5/SNX6 are required for CHC22 localization to ERGIC membranes independently of the ESCPE-1 complex. This interaction, together with a separate isoform-specific CHC22 N-terminal domain interaction with p115, constitutes a bipartite recruitment mechanism required for CHC22-mediated Golgi-bypass routing of GLUT4 to its storage compartment. Interference with either interaction inhibits GLUT4 targeting to the GSC. Co-immunoprecipitation, domain mapping, siRNA knockdown of SNX5/SNX6, GLUT4 trafficking assay, fluorescence microscopy The EMBO journal High 39160272
2024 SNX5 promotes antigen presentation in B cells by regulating actin-dependent plasma membrane remodeling and lysosomal trafficking to the immune synapse. SNX5 forms protrusions at the plasma membrane in steady state; B cells silenced for SNX5 exhibit enlarged lysosomes that fail to recruit to the synaptic membrane, reducing antigen extraction and presentation. siRNA silencing, fluorescence microscopy, live imaging, B cell immune synapse assay, lysosome trafficking assay Life science alliance Medium 39448266
2024 SNX5 directly binds Rab11a, increasing membrane accumulation of Rab11a GTPase. This interaction upregulates membrane content of LRP6, a cardiac hypertrophy regulator. siRNA knockdown of Rab11a antagonized the LRP6 membrane accumulation induced by SNX5 overexpression. SNX5 is downregulated in TAC-induced hypertrophic hearts; cardiac-specific overexpression of SNX5 improved cardiac function and reduced fibrosis. Interactome analysis, co-immunoprecipitation, fluorescence colocalization, membrane protein profiling, siRNA, AAV9-mediated cardiac-specific overexpression, echocardiography Journal of molecular and cellular cardiology Medium 38950816
2025 SNX5 plays a role in alpha-synuclein trafficking and toxicity. Knockdown of SNX5 protected human postmitotic neurons and mouse primary neurons against alpha-synuclein-induced toxicity. Extracellular and intracellular alpha-synuclein caused fragmentation of the trans-Golgi network, which was prevented by SNX5 knockdown, leading to confinement of alpha-synuclein in early endosomes. Genome-wide siRNA screen, independent siRNA validation, immunofluorescence microscopy, qPCR, Western blot, mouse primary neurons Translational neurodegeneration Medium 40457499
2025 SNX5 is a novel binding partner of MuRF2 and MuRF3 E3 ubiquitin ligases in muscle cells. The BAR domain of SNX5 mediates interaction with both MuRF2 and MuRF3. MuRF2 promotes ubiquitination of SNX5 at lysines 290 and 324, leading to proteasomal degradation, whereas MuRF3 counteracts this effect. SNX5 stabilizes PKA regulatory subunit RI-α within early endosomes; SNX5 knockout reduces RI-α stability, enhances PKA activity, increases HDAC5 degradation via autophagy-lysosomal pathway, upregulates myostatin via MEF2, and impairs myogenic differentiation. SILAC AP-MS, co-immunoprecipitation, domain mapping, ubiquitination assays, CRISPR-Cas9 KO, siRNA, endosome isolation, immunocytochemistry, qRT-PCR, Western blot Journal of cachexia, sarcopenia and muscle High 41077709
2025 SNX5 interacts with NCOA7-AS, a short isoform of Nuclear Receptor Coactivator 7 with antiviral activity against influenza A virus. Crystal structures of NCOA7-AS/SNX5 complexes revealed that the SNX5-interaction motif in NCOA7-AS is similar to known cargo interaction motifs. SNX5/6 are essential for NCOA7-AS antiviral activity against IAV. Critical residues for binding were identified by mutagenesis. Mass spectrometry, crystal structure, mutagenesis, siRNA knockdown, antiviral assay bioRxiv (preprint)preprint Medium bio_10.1101_2025.04.01.646557
2025 USP46 deubiquitinase interacts with and deubiquitinates SNX5, increasing its stability. Stabilized SNX5 promotes ferroptosis in ischemia-reperfusion-injured neuronal cells. Knockdown of SNX5 abolished the ferroptosis-promoting effect of USP46 in I/R-treated cells. Mass spectrometry (USP46 interactome), co-immunoprecipitation, deubiquitination assay, siRNA knockdown, ferroptosis assays in OGD/R model Experimental neurology Medium 39909216
2021 SNX5 overexpression blocked internalization and intracellular trafficking of CD44 in clear cell renal cell carcinoma (ccRCC) cells, preventing its lysosomal degradation and inhibiting TGF-β-induced EMT. KLF9 directly bound the SNX5 promoter and increased SNX5 transcription. Overexpression, knockdown, CD44 internalization assay, reporter assay for KLF9-SNX5 promoter, TGF-β stimulation, in vitro and in vivo proliferation/metastasis assays Molecular therapy oncolytics Medium 35024436
2025 SNX5 facilitates recycling of phosphorylated EGFR (p-EGFR) back to the plasma membrane to sustain EGFR signaling in osteoblast progenitors. Loss of Snx5 redirects EGFR trafficking toward late endosomes and lysosomal degradation, weakening EGFR signaling and abolishing mechanically-induced osteogenic enhancement. Multi-dataset screening, loss-of-function (Snx5 deficiency), EGFR trafficking assay, fluorescence microscopy, in vivo implant model International journal of oral science Medium 41714616
2025 SNX5 inhibits LRP5 internalization and promotes its recycling to the cell membrane in gastric cancer cells, preventing LRP5 from lysosomal degradation. Increased LRP5 membrane localization facilitated β-catenin stabilization and Wnt signaling pathway activation. SNX5 interaction with LRP5 was confirmed by co-immunoprecipitation. Co-immunoprecipitation, LRP5 internalization assay, membrane protein fractionation, β-catenin signaling assay, overexpression/knockdown Oncogene Medium 39922976
2025 Molecular dynamics and metadynamics simulations of the SNX1-SNX5 heterodimer reveal that SNX5-PXD engages in aromatic residue-rich π-π interactions with the CI-MPR cargo tail, with favorable binding free energy. SNX1-PXD drives membrane binding while SNX5-PXD contributes cargo recognition in a retromer-independent fashion. These computational findings are validated against cryo-EM structures of membrane-bound SNX1-SNX5. All-atom molecular dynamics simulation, metadynamics, dynamically triangulated surface mesoscopic simulation, comparison to cryo-EM structures Biophysical journal Low 41206513

Source papers

Stage 0 corpus · 26 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. Journal of cell science 212 17148574
1999 SNX5, a new member of the sorting nexin family, binds to the Fanconi anemia complementation group A protein. Biochemical and biophysical research communications 53 10600472
2008 A role for SNX5 in the regulation of macropinocytosis. BMC cell biology 49 18854019
2012 SNX5 is essential for efficient macropinocytosis and antigen processing in primary macrophages. Biology open 32 23213485
2015 miR-216a regulates snx5, a novel notch signaling pathway component, during zebrafish retinal development. Developmental biology 30 25645681
2008 The DHR1 domain of DOCK180 binds to SNX5 and regulates cation-independent mannose 6-phosphate receptor transport. Molecular biology of the cell 29 18596235
2021 Exosomal circRNA 0001445 promotes glioma progression through miRNA-127-5p/SNX5 pathway. Aging 25 33982667
2006 Snx5, as a Mind bomb-binding protein, is expressed in hematopoietic and endothelial precursor cells in zebrafish. FEBS letters 23 16857196
2021 SNX5 suppresses clear cell renal cell carcinoma progression by inducing CD44 internalization and epithelial-to-mesenchymal transition. Molecular therapy oncolytics 22 35024436
2017 Loss of renal SNX5 results in impaired IDE activity and insulin resistance in mice. Diabetologia 19 29080975
2022 SNX5 targets a monoamine transporter to the TGN for assembly into dense core vesicles by AP-3. The Journal of cell biology 9 35426896
2023 The association of lipid transfer protein VPS13A with endosomes is mediated by sorting nexin SNX5. Life science alliance 8 36977596
2019 SNX5 inhibits RLR-mediated antiviral signaling by targeting RIG-I-VISA signalosome. Biochemical and biophysical research communications 6 31806368
2022 Overexpression of lncRNA HOXA-AS2 promotes the progression of oral squamous cell carcinoma by mediating SNX5 expression. BMC molecular and cell biology 5 36528556
2024 CHC22 clathrin recruitment to the early secretory pathway requires two-site interaction with SNX5 and p115. The EMBO journal 3 39160272
2024 SNX5 promotes antigen presentation in B cells by dual regulation of actin and lysosomal dynamics. Life science alliance 3 39448266
2025 SNX5 facilitates the progression of gastric cancer by increasing the membrane localization of LRP5. Oncogene 2 39922976
2024 SNX5-Rab11a protects against cardiac hypertrophy through regulating LRP6 membrane translocation. Journal of molecular and cellular cardiology 2 38950816
2024 Moxibustion improves motor function by down-regulating SNX5 and inhibiting ferroptosis in neurons of corpus striatum in mice with Parkinson's disease. Zhen ci yan jiu = Acupuncture research 2 39020492
2025 Heliox alleviates ischemia-reperfusion-induced damage to neuronal cells by repressing the USP46-SNX5 Axis-triggered ferroptosis. Experimental neurology 1 39909216
2025 A genome-wide RNA interference screening reveals protectiveness of SNX5 knockdown in a Parkinson's disease cell model. Translational neurodegeneration 1 40457499
2025 The Novel MuRF2 Target SNX5 Regulates PKA Activity Through Stabilization of RI-α and Controls Myogenic Differentiation. Journal of cachexia, sarcopenia and muscle 1 41077709
2025 Division of labor in cargo and membrane recognition by SNX1-SNX5: Insights from multiscale modeling. Biophysical journal 1 41206513
2024 Noncanonical formation of SNX5 gene-derived circular RNA regulates cancer growth. Cell death & disease 1 39155279
2026 Implantation awakens peri-implant osteogenic potential via Snx5-EGFR axis-mediated mechanical transduction. International journal of oral science 0 41714616
2026 Hypermethylation‑induced silencing of ITGA4 promotes oral squamous cell carcinoma progression through SNX5 upregulation. Oncology reports 0 42028750