Affinage

SIDT2

SID1 transmembrane family member 2 · UniProt Q8NBJ9

Length
832 aa
Mass
94.5 kDa
Annotated
2026-06-10
43 papers in source corpus 23 papers cited in narrative 23 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

SIDT2 is a highly glycosylated, multi-pass lysosomal integral membrane protein that functions as a direct transporter of nucleic acids across the lysosomal membrane, mediating the macroautophagy-independent degradation of RNA (RNautophagy) and DNA (DNautophagy) (PMID:27046251, PMID:20965152, PMID:27846365). Substrate engagement is achieved through an arginine-rich motif (ARM) in its main cytosolic domain that directly binds RNA and DNA; disrupting this ARM abolishes RNautophagic activity, and the ARM acts synergistically with that of LAMP2C (PMID:31944164). Correct lysosomal delivery of SIDT2 depends on three cytosolic YxxΦ motifs that recruit the clathrin adaptor complexes AP-1 and AP-2, and this targeting is required for its transport function (PMID:28724756). Beyond the lysosome, SIDT2 transports internalized extracellular dsRNA from endocytic compartments into the cytoplasm to trigger antiviral innate immunity, with Sidt2-deficient mice showing impaired cytokine responses and reduced survival upon EMCV and HSV-1 infection (PMID:28916264), and it mediates cellular uptake of naked single-stranded oligonucleotides (gymnosis) and modulates the activity and lysosomal entrapment of therapeutic antisense oligonucleotides (PMID:28277980, PMID:36576400, PMID:39747556). Through its ARM-mediated binding to the expanded CAG-repeat HTT transcript, SIDT2 promotes degradation of mutant huntingtin and reduces polyQ aggregates in cell and mouse HD models (PMID:31944164, PMID:41736445). Across tissues, loss of SIDT2 impairs autophagosome–lysosome fusion and lysosomal acidification, producing lipid droplet accumulation, mitochondrial dysfunction, and organ pathology in liver, muscle, and kidney (PMID:29363559, PMID:34923568, PMID:33715196), and it contributes to insulin secretory granule exocytosis via NAADP-mediated calcium release from acidic compartments (PMID:23776622, PMID:26744456). Biallelic SIDT2 missense variants that disrupt RNA binding cause a human disorder with impaired autophagy, motor incoordination, and seizures recapitulating the knockout mouse brain phenotype (PMID:40541391).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2010 High

    Establishing where SIDT2 resides and its post-translational state was the necessary first step before any transport function could be assigned.

    Evidence Immunofluorescence, subcellular fractionation, and PNGase F deglycosylation

    PMID:20965152

    Open questions at the time
    • Did not define topology or number of transmembrane passes
    • No functional activity assigned
  2. 2013 High

    Whole-animal knockout first connected SIDT2 to a physiological process, revealing a requirement for insulin secretory granule exocytosis and glucose homeostasis.

    Evidence Global Sidt2 knockout mouse with glucose tolerance tests, islet secretion assays, and electron microscopy

    PMID:23776622

    Open questions at the time
    • Molecular mechanism linking SIDT2 to granule exocytosis unresolved
    • Did not connect phenotype to lysosomal transport activity
  3. 2015 Low

    An attempt to mechanistically link SIDT2 to the secretory machinery pointed to SNARE protein expression changes.

    Evidence Knockout mouse islet gene-expression panel and insulin secretion assays

    PMID:26884831

    Open questions at the time
    • Correlative mRNA changes only, no direct mechanistic link between SIDT2 and SNARE proteins
    • No protein-level or interaction evidence
  4. 2016 High

    The defining molecular function emerged: SIDT2 directly translocates RNA, and then DNA, across the lysosomal membrane, accounting for a large fraction of cellular RNA degradation independent of macroautophagy.

    Evidence Reciprocal gain/loss-of-function in isolated lysosomes (RNautophagy); ATP-dependent DNA uptake assays (DNautophagy)

    PMID:27046251 PMID:27846365

    Open questions at the time
    • Mechanism of translocation across the bilayer not resolved
    • DNautophagy shown by single lab
  5. 2016 Medium

    Pharmacological dissection placed SIDT2 in NAADP-mediated calcium release from acidic granules, linking its lysosomal role to the earlier insulin phenotype.

    Evidence Calcium imaging in Sidt2−/− primary β-cells with NAADP, bafilomycin A1, and other inhibitors

    PMID:26744456

    Open questions at the time
    • Does not establish whether SIDT2 directly conducts or gates calcium release
    • Single lab
  6. 2017 High

    The sorting logic and immune relevance of SIDT2 were defined: YxxΦ/AP-dependent lysosomal targeting underlies its degradative function, and it routes extracellular dsRNA to the cytoplasm for antiviral defense.

    Evidence YxxΦ mutagenesis with AP-1/AP-2 Co-IP and RNA degradation assays; Sidt2 knockout mouse viral challenge with cytokine assays

    PMID:28724756 PMID:28916264

    Open questions at the time
    • How the same protein switches between lysosomal degradation and endosome-to-cytosol delivery unclear
    • Cytosolic sensors activated downstream not defined in these findings
  7. 2017 Medium

    Additional transport behaviors were characterized — uptake of naked ssOligos (gymnosis) and, under heterologous overexpression, monovalent cation channel activity at the plasma membrane.

    Evidence siRNA/overexpression/single-residue mutagenesis with ssOligo uptake assay; whole-cell patch clamp in HEK293 overexpression

    PMID:27987306 PMID:28277980

    Open questions at the time
    • Channel activity measured under overexpression that mislocalizes protein to plasma membrane
    • Physiological relevance of cation conductance unestablished
  8. 2018 Medium

    Tissue-specific knockouts established that SIDT2 is broadly required for the late stage of autophagy, with loss blocking autophagosome maturation and causing lipid and aggregate accumulation in liver and muscle.

    Evidence Global and muscle-specific knockout mice with p62/LC3-II Western blot, electron microscopy, and β-oxidation/enzyme-activity controls

    PMID:29363559 PMID:29752955

    Open questions at the time
    • Mechanistic link between nucleic acid transport and autophagosome–lysosome fusion not resolved
    • Single lab per tissue
  9. 2019 Medium

    Genetic epistasis revealed a pro-tumorigenic role, with SIDT2 loss reducing tumor burden and causing dsRNA accumulation coupled to stress signaling and apoptosis.

    Evidence Sidt2 knockout in KrasG12D lung and Apcmin/+ intestinal tumor models with phospho-eIF2α/JNK and apoptosis readouts

    PMID:31546103

    Open questions at the time
    • Causal chain from dsRNA accumulation to tumorigenesis not fully dissected
    • Single lab
  10. 2020 High

    The substrate-binding determinant was localized to an arginine-rich motif in the cytosolic domain that directly binds nucleic acids and engages the expanded HTT transcript, providing a molecular handle for its degradative function.

    Evidence GST pulldown in vitro binding, ARM mutagenesis, cellular RNautophagy assays, and HTT aggregate Western blots

    PMID:31944164

    Open questions at the time
    • Structure of the ARM–RNA complex not determined
    • How ARM binding couples to membrane translocation unknown
  11. 2021 Medium

    A series of studies expanded SIDT2 into lysosome positioning, lipid handling, mitochondrial quality control, sterol transport, and ApoA1 secretion, broadening its functional footprint beyond nucleic acid transport.

    Evidence Kidney and muscle tissue-specific knockouts; CRAC-2 mutagenesis and Co-IP with ApoA1; dehydroergosterol uptake with a missense variant; miR-25/NOX4/ROS signaling in docetaxel-treated cells

    PMID:33715196 PMID:34233476 PMID:34863979 PMID:34923568 PMID:37830567

    Open questions at the time
    • Whether these activities share a common transport mechanism is unresolved
    • Several rest on single-lab Co-IP or single-method assays
  12. 2022 Medium

    An interactome and imaging study connected SIDT2 to microtubule-associated proteins and lysosome positioning, and to entrapment and activity of therapeutic antisense oligonucleotides.

    Evidence SIDT2 knockdown with PS-ASO co-localization imaging and MS-based interactome

    PMID:36576400

    Open questions at the time
    • Direct interaction with named motor/microtubule proteins not validated
    • Mechanism linking SIDT2 to lysosome positioning unknown
  13. 2025 Medium

    Human genetics and therapeutic modeling closed the loop: biallelic RNA-binding-disrupting variants cause a neurological disorder mirroring the knockout, and SIDT2 overexpression clears mutant huntingtin in HD models.

    Evidence Patient variant RNA-binding and fibroblast autophagy analysis with knockout mouse phenotyping; AAV-mediated SIDT2 overexpression in R6/2 mouse hypothalamus and neuronal cells; gapmer ASO domain-swap analysis

    PMID:39747556 PMID:40541391 PMID:41736445

    Open questions at the time
    • Disease established from a single patient study
    • Therapeutic durability and off-target consequences of SIDT2 overexpression unaddressed

Open questions

Synthesis pass · forward-looking unresolved questions
  • The unifying biophysical question — how SIDT2 physically translocates large nucleic acids and oligonucleotides across a membrane, and whether its diverse reported activities (cation conduction, sterol uptake, calcium release, ApoA1 binding) reflect one transport mechanism or distinct functions — remains unresolved.
  • No structure of SIDT2 or its transport pore
  • Transport stoichiometry and energetics undefined
  • Unclear whether lysosomal and plasma-membrane functions coexist physiologically

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005215 transporter activity 4 GO:0003677 DNA binding 2 GO:0003723 RNA binding 2 GO:0005198 structural molecule activity 1
Localization
GO:0005764 lysosome 2 GO:0005768 endosome 2 GO:0005886 plasma membrane 1
Pathway
R-HSA-9612973 Autophagy 3 R-HSA-8953854 Metabolism of RNA 2 R-HSA-168256 Immune System 1 R-HSA-9609507 Protein localization 1
Partners
AP1AP2APOA1LAMP2

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2016 SIDT2 is a transmembrane lysosomal integral membrane protein that mediates direct RNA translocation across the lysosomal membrane during RNautophagy; gain- and loss-of-function studies with isolated lysosomes showed SIDT2 knockdown inhibited ~50% of total cellular RNA degradation independently of macroautophagy. Gain- and loss-of-function studies with isolated lysosomes; subcellular fractionation; immunofluorescence with lysosomal markers Autophagy High 27046251
2010 SIDT2 is a highly glycosylated lysosomal integral membrane protein; its lysosomal localization was determined by immunofluorescence with lysosomal markers and subcellular fractionation, and its apparent molecular weight (~120–130 kDa) decreases to ~95 kDa after PNGase F digestion, confirming extensive N-glycosylation. Immunofluorescence, subcellular fractionation, PNGase F digestion, Western blot Biochemical and biophysical research communications High 20965152
2016 SIDT2 also mediates DNA translocation during DNautophagy, the direct uptake of DNA by lysosomes in an ATP-dependent manner. Gain- and loss-of-function studies with isolated lysosomes Autophagy Medium 27846365
2017 SIDT2 is required for transport of internalized extracellular dsRNA from endocytic compartments into the cytoplasm for innate immune activation; Sidt2-deficient mice show impaired antiviral cytokine production and reduced survival upon EMCV and HSV-1 infection. Sidt2 knockout mouse model; virus challenge (EMCV, HSV-1); cytokine production assays; extracellular dsRNA treatment Immunity High 28916264
2017 Three cytosolic YxxΦ motifs in SIDT2 are required for its lysosomal localization; SIDT2 interacts with adaptor protein complexes AP-1 and AP-2, and this lysosomal targeting is necessary for its function in RNautophagy. Overexpression of SIDT2 substantially increases endogenous RNA degradation at the cellular level. Mutagenesis of YxxΦ motifs; co-immunoprecipitation with AP-1 and AP-2; live-cell imaging; RNA degradation assays Journal of cell science High 28724756
2017 SIDT2 mediates gymnosis — the uptake of naked single-stranded oligonucleotides (ssOligos) into living cells; SIDT2 knockdown significantly reduced ssOligo uptake, overexpression enhanced it, and a single amino acid mutation in SIDT2 abolished the enhancing effect. siRNA knockdown; overexpression; single amino acid mutagenesis; fluorescent ssOligo uptake assay RNA biology Medium 28277980
2020 SIDT2 directly binds RNA and DNA through an arginine-rich motif (ARM) in its main cytosolic domain; disruption of this ARM dramatically impairs SIDT2-mediated RNautophagic activity. SIDT2 ARM also mediates interaction with the CAG repeat-containing HTT exon 1 transcript, and overexpression of SIDT2 promoted HTT mRNA degradation and reduced polyQ-expanded HTT aggregates. SIDT2 and LAMP2C ARM motifs act synergistically in RNautophagy. In vitro binding assays (GST pulldown); ARM mutagenesis; cellular RNautophagy activity assays; Western blot for HTT aggregates; co-expression/synergy experiments Autophagy High 31944164
2017 SIDT2 overexpressed in HEK293 cells reaches the plasma membrane and functions as a spontaneous, non-inactivating monovalent cation channel, causing cell depolarization upon sodium addition; strong overexpression leads to significant reduction/loss of detectable lysosomes. Heterologous overexpression in HEK293 cells; whole-cell patch clamp electrophysiology; lysosome detection assays FEBS letters Medium 27987306
2013 Sidt2-deficient (knockout) mice exhibit glucose intolerance, decreased serum insulin, hypertrophic islets with accumulation of insulin secretory granules, and impaired glucose-stimulated insulin secretion; isolated Sidt2−/− islets produce less insulin upon glucose or KCl stimulation, indicating a role for Sidt2 in insulin secretory granule exocytosis. Global Sidt2 knockout mouse; glucose tolerance tests; isolated islet insulin secretion assays; electron microscopy; Western blot; immunofluorescence PloS one High 23776622
2016 SIDT2 is involved in NAADP-mediated calcium release from intracellular acidic compartments (insulin secretory granules) in pancreatic β-cells; Sidt2−/− β-cells show reduced glucose-induced [Ca2+]i peak, which is normalized by exogenous NAADP application, while bafilomycin A1 treatment equalized [Ca2+]i responses between Sidt2−/− and WT cells. Primary β-cell culture from Sidt2−/− mice; calcium imaging; pharmacological inhibitors (ryanodine, 2-APB, bafilomycin A1, NAADP); patch clamp for KATP and KV currents Journal of molecular endocrinology Medium 26744456
2018 Hepatocyte-specific effects of Sidt2 deficiency include lipid droplet accumulation and impaired hepatic β-oxidation with decreased autophagic flux; Sidt2−/− mice show block of autophagosome maturation as evidenced by elevated p62 and LC3-II and accumulation of autophagolysosomes by electron microscopy. Global Sidt2 knockout mouse; serum β-hydroxybutyrate measurement; Western blot for p62 and LC3-II; electron microscopy; primary hepatocyte autophagic flux assays Journal of lipid research Medium 29363559
2018 Skeletal muscle-specific Sidt2 knockout mice develop a muscular dystrophy-like phenotype with accumulation of autophagolysosomes, increased LC3-II, p62, ubiquitinated aggregates, and LAMP2-positive vacuoles, while proteasome and lysosomal soluble enzyme activities were unimpaired, indicating a specific role for Sidt2 in the late stage of autophagy in muscle. Muscle-specific Sidt2 knockout mouse (Cre/LoxP); morphologic and functional studies; Western blot; immunostaining; genechip RNA expression analysis; proteasome activity assay; lysosomal enzyme activity assay Metabolism: clinical and experimental Medium 29752955
2021 Sidt2 deletion in kidney (Sidt2−/− mice) impairs lysosomal function (decreased acidic lysosomes, reduced acid hydrolase activity, elevated lysosomal pH), blocks autophagosome–lysosome fusion and autolysosome degradation, and leads to structural and functional kidney damage (basement membrane thickening, podocyte foot process fusion, proteinuria). Sidt2 knockout mouse; LysoTracker staining; lysosomal enzyme activity assays; LC3-II/p62 Western blot; immunofluorescence for autophagosome-lysosome fusion; Ad-mcherry-GFP-LC3B; chloroquine experiments; electron microscopy Cell death & disease Medium 34923568
2021 Sidt2 deletion in skeletal muscle reduces expression of mitochondrial fusion protein Mfn2, fission protein Drp1, and PGC1-α, blocks autophagosome–lysosome fusion, impairs clearance of damaged mitochondria, and causes accumulation of structurally abnormal mitochondria with reduced muscle tolerance. Skeletal muscle-selective Sidt2 knockout mice; Western blot for Mfn2, Drp1, PGC1-α; autophagy flux assays; electron microscopy; functional muscle tests FASEB journal Medium 33715196
2019 SIDT2 promotes tumor development; Sidt2−/− mice with KrasG12D activation develop significantly fewer lung tumors, and loss of SIDT2 delays intestinal tumor development in Apcmin/+ mice; in the intestine, SIDT2 loss leads to dsRNA accumulation associated with increased eIF2α and JNK phosphorylation and elevated apoptosis. Sidt2 knockout in KrasG12D lung adenocarcinoma model and Apcmin/+ intestinal cancer model; tumor counting; phospho-eIF2α and phospho-JNK Western blot; apoptosis assays iScience Medium 31546103
2021 SIDT2 forms a complex with apolipoprotein A1 (ApoA1) requiring the second CRAC motif (CRAC-2) in SIDT2; overexpression of SIDT2 enhances ApoA1 secretion from HepG2 hepatocytes, and this effect is abolished when the CRAC-2 domain is mutated. Co-immunoprecipitation; CRAC-2 domain mutagenesis; ApoA1 secretion assay in HepG2 cells Cells Medium 37830567
2021 SIDT2/Val636Ile missense variant shows increased uptake of the cholesterol analog dehydroergosterol compared to wild-type in vitro, indicating that this variant alters SIDT2's sterol transport function. In vitro site-directed mutagenesis; dehydroergosterol (fluorescent cholesterol analog) uptake assay Arteriosclerosis, thrombosis, and vascular biology Medium 34233476
2022 SIDT2 regulates lysosome cellular location, potentially via interaction with microtubule-related proteins; SIDT2 is required for proper co-localization between phosphorothioate antisense oligonucleotides (PS-ASOs) and lysosomes, and SIDT2 loss reduces PS-ASO lysosomal entrapment and increases ASO activity. SIDT2 knockdown; PS-ASO co-localization imaging; SIDT2 interactome (MS-based identification of microtubule-related binding partners); lysosome positioning assays Nucleic acid therapeutics Medium 36576400
2021 In docetaxel-treated cancer cells, SIDT2 expression is upregulated and mediates lysosomal degradation of miR-25, which in turn increases NOX4 expression; this activates ROS/JNK signaling leading to HuR phosphorylation and TNF-α mRNA stabilization, ultimately causing TNF-α-dependent apoptosis. siRNA knockdown of SIDT2; chloroquine (lysosome inhibitor) pretreatment; miR-25 quantification; NOX4/ROS/JNK/HuR Western blot; cell viability and apoptosis assays Biochemical pharmacology Medium 34863979
2025 Biallelic SIDT2 missense variants (p.Arg529Trp, p.Arg678Trp) in a human patient disrupted SIDT2's ability to interact with RNA; patient fibroblasts showed impaired autophagy with abnormal accumulation of autophagy markers, mimicking Sidt2 knockout mouse brain phenotypes including motor incoordination and seizures. Functional RNA-binding studies of patient variants; patient fibroblast autophagy marker analysis; Sidt2 knockout mouse neurological phenotyping; brain expression analysis Journal of medical genetics Medium 40541391
2025 SIDT2 overexpression via AAV vectors in the lateral hypothalamus of R6/2 HD mice reduced mutant huntingtin (mHTT) inclusions; in a neuronal cell model, SIDT2 overexpression reduced soluble and insoluble mHTT exon 1 protein levels, consistent with its known ARM-mediated binding to the expanded CAG repeat in mHTT transcript. AAV-mediated SIDT2 overexpression in R6/2 mouse hypothalamus; mHTT inclusion quantification by immunohistochemistry; neuronal cell model overexpression with Western blot for mHTT Brain pathology (Zurich, Switzerland) Medium 41736445
2015 Sidt2 deficiency in islets correlates with significantly decreased expression of SNARE proteins synaptopodin 1 (synap1) and synaptopodin 3 (synap3), suggesting that Sidt2 regulates insulin secretory granule exocytosis via SNARE-dependent mechanisms. Sidt2 knockout mouse; gene expression analysis (13-gene panel); in vivo and in vitro insulin secretion assays International journal of clinical and experimental pathology Low 26884831
2025 SIDT2 (expressed in human cell lines) enhances knockdown activity of gapmer ASOs and promotes their endosomal escape into the cytosol; a specific region in SIDT2 (identified by chimeric SIDT2/SIDT1 protein analysis) is critical for this activity and distinguishes SIDT2 from SIDT1. Overexpression of SIDT1 and SIDT2 in human cell lines; gapmer ASO knockdown activity assays; chimeric protein domain-swap analysis Scientific reports Medium 39747556

Source papers

Stage 0 corpus · 43 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 SIDT2 Transports Extracellular dsRNA into the Cytoplasm for Innate Immune Recognition. Immunity 107 28916264
2016 Lysosomal putative RNA transporter SIDT2 mediates direct uptake of RNA by lysosomes. Autophagy 84 27046251
2010 SID1 transmembrane family, member 2 (Sidt2): a novel lysosomal membrane protein. Biochemical and biophysical research communications 57 20965152
2020 Cytosolic domain of SIDT2 carries an arginine-rich motif that binds to RNA/DNA and is important for the direct transport of nucleic acids into lysosomes. Autophagy 45 31944164
2016 Lysosomal membrane protein SIDT2 mediates the direct uptake of DNA by lysosomes. Autophagy 45 27846365
2017 SIDT2 mediates gymnosis, the uptake of naked single-stranded oligonucleotides into living cells. RNA biology 38 28277980
2018 Sidt2 regulates hepatocellular lipid metabolism through autophagy. Journal of lipid research 34 29363559
2013 Impaired glucose tolerance in a mouse model of sidt2 deficiency. PloS one 34 23776622
2021 Sidt2 is a key protein in the autophagy-lysosomal degradation pathway and is essential for the maintenance of kidney structure and filtration function. Cell death & disease 31 34923568
2016 Spontaneous nonalcoholic fatty liver disease and ER stress in Sidt2 deficiency mice. Biochemical and biophysical research communications 31 27233614
2019 SIDT2 RNA Transporter Promotes Lung and Gastrointestinal Tumor Development. iScience 23 31546103
2021 Long non-coding RNA LIFR-AS1 suppressed the proliferation, angiogenesis, migration and invasion of papillary thyroid cancer cells via the miR-31-5p/SIDT2 axis. Cell cycle (Georgetown, Tex.) 22 34781815
2015 Lysosomal integral membrane protein Sidt2 plays a vital role in insulin secretion. International journal of clinical and experimental pathology 21 26884831
2021 Docetaxel-triggered SIDT2/NOX4/JNK/HuR signaling axis is associated with TNF-α-mediated apoptosis of cancer cells. Biochemical pharmacology 20 34863979
2017 Lysosomal targeting of SIDT2 via multiple YxxΦ motifs is required for SIDT2 function in the process of RNautophagy. Journal of cell science 19 28724756
2018 Multiple genotype-phenotype association study reveals intronic variant pair on SIDT2 associated with metabolic syndrome in a Korean population. Human genomics 18 30382898
2016 SIDT2 is involved in the NAADP-mediated release of calcium from insulin secretory granules. Journal of molecular endocrinology 17 26744456
2011 Cloning, characterization, and biological function analysis of the SidT2 gene from Siniperca chuatsi. Developmental and comparative immunology 17 21334374
2021 Genome-Wide Association Study Identifies a Functional SIDT2 Variant Associated With HDL-C (High-Density Lipoprotein Cholesterol) Levels and Premature Coronary Artery Disease. Arteriosclerosis, thrombosis, and vascular biology 16 34233476
2020 Effect of sidt2 Gene on Cell Insulin Resistance and Its Molecular Mechanism. Journal of diabetes research 14 32964053
2018 Skeletal muscle-specific Sidt2 knockout in mice induced muscular dystrophy-like phenotype. Metabolism: clinical and experimental 14 29752955
2018 Changes of lysosomal membrane permeabilization and lipid metabolism in sidt2 deficient mice. Experimental and therapeutic medicine 14 29896245
2017 Identification of Sidt2 as a lysosomal cation-conducting protein. FEBS letters 13 27987306
2021 The lysosomal membrane protein Sidt2 is a vital regulator of mitochondrial quality control in skeletal muscle. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 11 33715196
2021 Pathology-associated change in levels and localization of SIDT2 in postmortem brains of Parkinson's disease and dementia with Lewy bodies patients. Neurochemistry international 11 34800582
2023 Amsacrine downregulates BCL2L1 expression and triggers apoptosis in human chronic myeloid leukemia cells through the SIDT2/NOX4/ERK/HuR pathway. Toxicology and applied pharmacology 10 37451322
2020 The Effects of Sidt2 on the Inflammatory Pathway in Mouse Mesangial Cells. Mediators of inflammation 10 32565723
2018 Gene-based association study for lipid traits in diverse cohorts implicates BACE1 and SIDT2 regulation in triglyceride levels. PeerJ 10 29404214
2022 Effects of SIDT2 on the miR-25/NOX4/HuR axis and SIRT3 mRNA stability lead to ROS-mediated TNF-α expression in hydroquinone-treated leukemia cells. Cell biology and toxicology 9 35302183
2022 The functions of SID1 transmembrane family, member 2 (Sidt2). The FEBS journal 7 36176242
2024 Dihydromyricetin Improves Myocardial Functioning by Influencing Autophagy Through SNHG17/Mir-34a/SIDT2 Axis. Current molecular pharmacology 6 39976027
2023 Interaction between SIDT2 and ABCA1 Variants with Nutrients on HDL-c Levels in Mexican Adults. Nutrients 6 36678241
2020 The Variant rs1784042 of the SIDT2 Gene is Associated with Metabolic Syndrome through Low HDL-c Levels in a Mexican Population. Genes 6 33066450
2023 SIDT2 Associates with Apolipoprotein A1 (ApoA1) and Facilitates ApoA1 Secretion in Hepatocytes. Cells 5 37830567
2022 SIDT2 Inhibits Phosphorothioate Antisense Oligonucleotide Activity by Regulating Cellular Localization of Lysosomes. Nucleic acid therapeutics 5 36576400
2023 [Lysosomal membrane protein Sidt2 knockout induces apoptosis of human hepatocytes in vitro independent of the autophagy-lysosomal pathway]. Nan fang yi ke da xue xue bao = Journal of Southern Medical University 3 37202201
2025 Multispanning membrane protein SIDT2 increases knockdown activity of gapmer antisense oligonucleotides. Scientific reports 2 39747556
2025 Sidt2 ameliorates TNF-α-induced apoptosis and inflammation by promoting autophagic flux via p65 signaling. International immunopharmacology 2 40885088
2021 [Lysosomal membrane protein Sidt2 deletion impairs autophagy in human hepatocytes]. Nan fang yi ke da xue xue bao = Journal of Southern Medical University 2 34549712
2025 Biallelic SIDT2 loss-of-function in a child with cerebellar ataxia and lysosomal dysfunction mimics impairment of SIDT2 in mice. Journal of medical genetics 1 40541391
2026 The DNA/RNA autophagy protein SIDT2 as a novel neuropathological hallmark in Huntington disease. Brain pathology (Zurich, Switzerland) 0 41736445
2025 NIR-II Imaging Guided Accurate Identification of Paraspinal Muscle Degeneration Through Targeting the Lysosomal Membrane Protein Sidt2. International journal of nanomedicine 0 40551976
2025 Sidt2 inhibits islet β-cell dedifferentiation by regulating insulin secretion. The Journal of biological chemistry 0 40749831

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