| 2008 |
TRIM22 inhibits HIV-1 particle release by targeting HIV Gag, disrupting its trafficking to the plasma membrane; the RING domain catalytic residues Cys15 and Cys18 are required for this antiviral activity. TRIM22 does not block MLV or EIAV Gag particle release, indicating specificity for HIV Gag. |
RNAi knockdown, overexpression, virus-like particle budding assay, mutational analysis of RING domain (C15A/C18A), fluorescence microscopy of Gag localization |
PLoS pathogens |
High |
18389079
|
| 2008 |
TRIM22 is a functional E3 ubiquitin ligase that catalyzes self-ubiquitylation in vitro in combination with E2 enzyme UbcH5B, dependent on its RING finger domain; TRIM22 also undergoes self-ubiquitylation in vivo and is targeted for proteasomal degradation via poly-ubiquitin chains. TRIM22 localizes to the nucleus. |
In vitro ubiquitylation assay with UbcH5B, in vivo ubiquitylation in 293T cells, proteasome inhibitor stabilization assay, subcellular fractionation/localization |
Biochemical and biophysical research communications |
High |
18656448
|
| 2009 |
TRIM22 E3 ubiquitin ligase activity is required for antiviral protection against encephalomyocarditis virus (ECMV); TRIM22 interacts with the viral 3C protease (3C^PRO) and mediates its ubiquitination. A RING domain deletion mutant abolishes both E3 activity and antiviral effect. |
Antiviral protection assay in HeLa cells, co-immunoprecipitation of TRIM22 with 3C^PRO, ubiquitination assay, RING deletion mutant analysis |
The Journal of general virology |
High |
19218198
|
| 2011 |
TRIM22 inhibits HIV-1 LTR-driven transcription independently of its E3 ubiquitin ligase activity, Tat transactivation, and NF-κB binding sites in the LTR. Nuclear TRIM22 suppresses basal and phorbol ester-induced HIV-1 transcription. |
Stable TRIM22 knockdown in U937 cells, TRIM22 transduction in permissive cells, LTR-luciferase reporter assays with NF-κB site deletion constructs, RING mutant (E3-dead) analysis |
Journal of virology |
High |
21345949
|
| 2013 |
TRIM22 restricts influenza A virus (IAV) replication by interacting with the viral nucleoprotein (NP) and promoting its polyubiquitination and proteasome-dependent degradation. |
shRNA knockdown, overexpression in MDCK cells, Co-IP of TRIM22 with NP, ubiquitination assay, proteasome inhibitor rescue, viral titer measurement |
Journal of virology |
High |
23408607
|
| 2011 |
TRIM22 activates NF-κB in a dose-dependent manner; both the N-terminal RING domain and C-terminal SPRY domain are required for NF-κB activation. TRIM22 overexpression induces pro-inflammatory cytokine secretion in U937 macrophages in an NF-κB-dependent manner. |
NF-κB luciferase reporter assay, EMSA, domain deletion mutants, cytokine ELISA |
Biochemical and biophysical research communications |
Medium |
21651891
|
| 2015 |
TRIM22 inhibits HIV-1 LTR-driven transcription by preventing Sp1 binding to the viral promoter; TRIM22 does not interact directly with Sp1 but blocks Sp1 binding as shown by protein-DNA pulldown and chromatin immunoprecipitation. |
Reporter assays with Sp1-binding-site deletion constructs in 293T cells, TRIM22 KD in SupT1 T cells with HIV replication assay, protein-DNA pulldown, chromatin immunoprecipitation (ChIP) |
Retrovirology |
High |
26683615
|
| 2015 |
TRIM22 ubiquitinates HCV NS5A protein in a concentration-dependent manner, and TRIM22 expression inhibits HCV replication; siRNA-mediated TRIM22 knockdown diminishes IFNα-induced anti-HCV function. |
TRIM22 overexpression and siRNA knockdown in Huh-7 cells, HCV replication assay, NS5A ubiquitination assay |
Cellular & molecular immunology |
Medium |
25683609
|
| 2013 |
TRIM22 inhibits the TRAF6-stimulated NF-κB pathway by interacting with and degrading TAB2 in a RING domain-dependent manner; TRIM22 also decreases TRAF6 self-ubiquitination. |
NF-κB reporter assay, Co-IP of TRIM22 with TAB2, TAB2 degradation assay with RING deletion mutant, TRAF6 ubiquitination assay |
Virologica Sinica |
Medium |
23818111
|
| 2004 |
TRIM22 (Staf50) is a direct p53 target gene; a functional p53-response element in intron 1 mediates direct p53 binding (shown by EMSA) and transactivation; p53-family member p73 also transactivates via this element. Ectopic TRIM22 expression reduces clonogenic growth of U937 leukemic cells. |
cDNA microarray, cycloheximide chase (independence of de novo protein synthesis), EMSA, luciferase reporter assay with intron 1 p53-RE, ectopic expression clonogenic assay |
Oncogene |
High |
15064739
|
| 2009 |
Human and rhesus TRIM22 localize to different subcellular compartments, and this difference maps to the B30.2/SPRY domain; amino acid changes in variable loops VL1 and VL3 of the B30.2 domain are responsible for the species-specific subcellular localization differences. |
Fluorescence microscopy of GFP-tagged constructs, domain swap/chimeric protein experiments, mutational analysis of VL1 and VL3 |
Immunogenetics |
Medium |
19212762
|
| 2009 |
Endogenous TRIM22 colocalizes with centrosomes independently of cell cycle phase in primary human mononuclear cells and U2OS cells, and this colocalization is independent of the microtubule network. |
Immunofluorescence of endogenous TRIM22 with centrosome markers, microtubule depolymerization experiment, cell cycle staging |
Experimental cell research |
Medium |
20006605
|
| 2012 |
TRIM22 directly or indirectly interacts with translation initiation factor eIF4E and inhibits eIF4E binding to eIF4G, thereby disrupting eIF4F complex assembly and repressing cap-dependent translation of specific mRNAs including IRF-7C. |
Co-immunoprecipitation of TRIM22 with eIF4E, eIF4G binding competition assay, luciferase reporter assay, radiolabelled methionine incorporation assay |
Biology of the cell |
Medium |
22509910
|
| 2015 |
TRIM22 activates the noncanonical NF-κB pathway by interacting with IKKα (but not IKKβ) via its RING and SPRY domains, increasing IKKα levels and phosphorylation, and inducing p100 processing to p52. |
Co-immunoprecipitation, co-localization, Western blot for p100/p52 processing and IKKα phosphorylation, domain deletion mutants |
Journal of receptor and signal transduction research |
Medium |
25510414
|
| 2016 |
TRIM22 variants disrupt the ability of TRIM22 to regulate NOD2-dependent activation of IFN-β signaling and NF-κB, establishing TRIM22 as a regulator of the NOD2 signaling pathway in a disease context (very-early-onset IBD). |
Whole-exome sequencing, functional studies in primary patient cells and cell culture showing disrupted NOD2/IFN-β/NF-κB signaling by TRIM22 variants |
Gastroenterology |
Medium |
26836588
|
| 2020 |
TRIM22 promotes NF-κB signaling in GBM by: (1) binding IκBα and accelerating its degradation via K48-linked ubiquitination; (2) forming a complex with IKKγ and promoting K63-linked ubiquitination leading to IKKα/β and IκBα phosphorylation. RING domain E3 ligase activity is required for these effects. A non-phosphorylatable IκBα mutant (srIκBα) blocks TRIM22 growth-promoting activity. |
Co-immunoprecipitation, K48/K63-linked ubiquitination assays, Cas9-sgRNA knockout, RING mutant (C15/18A) and deletion analysis, NF-κB luciferase reporter, orthotopic xenograft model |
Cell death and differentiation |
High |
32814880
|
| 2022 |
TRIM22 promotes proteasomal degradation of NRF2 via E3 ligase-dependent ubiquitination that is independent of KEAP1, reducing intracellular antioxidant capacity and activating ROS/AMPK/mTOR/autophagy signaling to induce autophagic cell death in osteosarcoma. |
Co-immunoprecipitation of TRIM22 with NRF2, ubiquitination assay, E3 ligase mutant analysis, ROS measurement, AMPK/mTOR pathway Western blot, in vitro and in vivo gain/loss-of-function with rescue by NRF2 manipulation or NAC/3-MA |
Redox biology |
High |
35636015
|
| 2022 |
TRIM22 suppresses Zika virus (ZIKV) replication by interacting with viral NS1 and NS3 proteins and promoting their ubiquitination and proteasomal degradation; the SPRY domain mediates protein interaction and the RING domain mediates degradation. TRIM22 also inhibits dengue and yellow fever virus. |
Co-immunoprecipitation, ubiquitination assay, domain deletion analysis (SPRY and RING), overexpression and TRIM22 KO cell infectivity assay, proteasome inhibitor rescue |
Cell & bioscience |
High |
36042495
|
| 2024 |
TRIM22 E3 ubiquitin ligase promotes proteasomal degradation of SARS-CoV-2 NSP8 via K48-type ubiquitination at Lys97, thereby restricting viral replication; TRIM22 expression is induced by interferon signaling upon SARS-CoV-2 infection. |
Co-immunoprecipitation of TRIM22 with NSP8, K48-ubiquitination assay with site-specific Lys97 mutation, TRIM22 overexpression and knockdown viral replication assay |
mBio |
High |
38275298
|
| 2023 |
TRIM22 induces cellular senescence in hepatocellular carcinoma by targeting PHLPP2 for proteasomal degradation via the SPRY domain binding PHLPP2's C-terminal IKKβ-phosphorylated domain; PHLPP2 degradation activates AKT-p53-p21 signaling leading to senescence. |
Co-immunoprecipitation with domain mapping, ubiquitination assay, IKKβ phosphorylation analysis, AKT/p53/p21 Western blot, cellular senescence assays (β-galactosidase, SAHF), p53 ChIP for TRIM22 promoter |
Cell death & disease |
High |
38199981
|
| 2023 |
TRIM22 promotes GBM proliferation by activating MAPK signaling; it binds Raf-1 (a negative regulator) via CC and SPRY domains and accelerates Raf-1 degradation by K48-linked ubiquitination (interaction requires Raf-1 C1D domain). TRIM22 also binds the SPHK2 gene at exon 2 to regulate SPHK2 transcription. |
Co-immunoprecipitation with domain mapping, K48-ubiquitination assay, ERK1/2 luciferase reporter, TRIM22 KO and OE, RING domain and NLS deletion mutants, in vivo xenograft |
Experimental & molecular medicine |
Medium |
37258577
|
| 2015 |
TRIM22 ubiquitinates FoxO4 and targets it for degradation via the autophagosomal-lysosomal (not ubiquitin-proteasome) pathway; this antagonizes FoxO4's role in promoting IFN-β expression downstream of TLR3/RIG-I activation. TRIM22 knockdown sensitizes cells to dsRNA-induced caspase-dependent apoptosis and suppresses Bcl-2. |
TRIM22 KD with poly(I:C) stimulation, FoxO4 KD, IFN-β reporter assay, assessment of FoxO4 protein levels, apoptosis assay (caspase activation), Bcl-2 Western blot |
Journal of interferon & cytokine research |
Medium |
26237181
|
| 2017 |
HBV X protein (HBx) suppresses TRIM22 transcription through a single CpG methylation in the TRIM22 5'-UTR, which reduces IRF-1 binding affinity to the TRIM22 promoter, thereby enabling HBV to evade innate immune restriction. |
LC-MS/MS proteomics, bisulfite sequencing for CpG methylation, IRF-1 binding assay, mouse model, primary human hepatocytes |
Gut |
High |
28341749
|
| 2011 |
BRG1 (chromatin remodeling ATPase) is required for IFN-γ-induced TRIM22 expression; BRG1 deficiency does not impair IFN-γ-induced IRF-1 expression but blocks IRF-1 access to the TRIM22 promoter; BRG1 ATPase domain is required for TRIM22 induction and IRF-1 recruitment. |
BRG1-deficient SW-13 cell line with BRG1 reconstitution, ChIP of IRF-1 at TRIM22 promoter, BRG1 ATPase domain mutant |
Biochemical and biophysical research communications |
Medium |
21683060
|
| 2013 |
p300, but not PCAF, functions as a transcriptional co-activator of IRF-1 for IFN-γ-induced TRIM22 expression independently of p300's histone acetyltransferase activity; p300 is required for RNA polymerase II recruitment to the TRIM22 promoter. |
In vitro DNA affinity binding assay, ChIP of p300 and RNA Pol II at TRIM22 promoter, p300 overexpression and knockdown, HAT-dead p300 mutant |
European journal of immunology |
Medium |
23670564
|
| 2015 |
TRIM22 is a progesterone-receptor (PR) direct target gene; PR binds a progesterone response element (PRE) in the TRIM22 promoter region (-25 to -11 bp upstream of exon 1) in a hormone-dependent manner, and this PRE has enhancer activity. |
ChIP of PR at TRIM22 PRE, luciferase reporter assay for PRE activity, PR-stable Ishikawa cell clones, hormone-dependent TRIM22 expression |
The Journal of steroid biochemistry and molecular biology |
Medium |
26316153
|
| 2019 |
TRIM22 maintains HIV-1 proviral latency in T cell lines; TRIM22 knockdown accelerates reactivation of a dox-controlled HIV-1 in SupT1 cells and potentiates HIV-1 expression in ACH-2 and J-Lat 10.6 cell lines upon TNF-α or HDAC inhibitor stimulation. |
TRIM22 knockdown in T cell lines, dox-controlled HIV-1 replication system, TNF-α/HDACi stimulation, HIV-1 p24 and luciferase readouts |
Virus research |
Medium |
31136823
|
| 2019 |
TRIM22 interacts with PRRSV nucleocapsid (N) protein through its SPRY domain; the NLS2 motif of N protein is involved in the interaction with TRIM22. The NLS (nuclear localization signal) and SPRY domain of TRIM22 are both required for inhibition of PRRSV replication; however, PRRSV N protein levels are not altered by TRIM22, whereas N proteins from related arteriviruses (SHFV, EAV, LDV) are reduced by TRIM22 overexpression. |
Co-IP, TRIM22 domain deletion constructs (ΔSPRY, ΔNLS), ectopic expression and RNAi in MARC-145 cells, viral titer measurement |
Virus genes |
Medium |
31375995
|
| 2021 |
TRIM22 restricts HSV-1 replication by increasing histone occupancy and heterochromatin on viral immediate-early gene promoters, thereby reducing viral IE gene expression; this represents an epigenetic restriction mechanism independent of ICP0-mediated degradation. |
TRIM22 KO and overexpression, ChIP for histone occupancy and heterochromatin marks at viral IE promoters, ICP0-null and wild-type virus comparison, viral gene expression analysis |
PLoS pathogens |
High |
33524065
|
| 2023 |
TRIM22 promotes autophagosome-lysosome fusion by mediating the association of GABARAP family proteins with PLEKHM1, independently of its E3 ubiquitin ligase activity; a TRIM22 variant associated with familial Alzheimer disease interferes with this function and impairs autophagic clearance. |
Co-IP, proximity ligation assay, TRIM22 KO with autophagy flux assay, E3 ligase-dead mutant analysis, Alzheimer variant functional testing in cells |
Autophagy |
High |
38009729
|
| 2021 |
TRIM22 promotes PRRSV N protein degradation through the lysosomal pathway by interacting with LC3; PRRSV miR-376b-3p directly targets TRIM22 to impair its anti-PRRSV activity. |
Co-IP of TRIM22 with PRRSV N protein and LC3, lysosomal pathway inhibitor experiments, miRNA target validation, viral replication assay |
Journal of virology |
Medium |
34757838
|
| 2017 |
TRIM22 mediates apoptosis in monocytes by promoting Bak expression and oligomerization; both the RING and SPRY domains are required. TRIM22 overexpression activates caspase-9 and caspase-3. |
TRIM22 overexpression in THP-1 and primary monocytes, domain deletion mutants (ΔRING, ΔSPRY), caspase activation assay, Bak oligomerization analysis by native PAGE/fractionation |
Scientific reports |
Medium |
28079123
|
| 2022 |
TRIM22 forms a complex with NT5C2 in GBM and differentially regulates RIG-I ubiquitination: TRIM22 promotes K63-linked ubiquitination of RIG-I while NT5C2 promotes K48-linked ubiquitination, regulating the RIG-I/NF-κB/CCAR1 signaling axis. |
Co-IP, K48/K63-specific ubiquitination assays, TRIM22 KO with RIG-I ubiquitination readout, luciferase reporter, in vivo xenograft |
Molecular therapy oncolytics |
Medium |
36159777
|
| 2024 |
TRIM22 interacts with PHLPP2 (AKT phosphatase) and induces its proteasomal degradation, leading to AKT activation and cellular senescence via AKT-p53-p21 signaling; IKKβ-mediated phosphorylation of PHLPP2's C-terminal domain is a prerequisite for TRIM22-SPRY-domain-mediated recognition. |
Co-IP with SPRY domain mapping, ubiquitination assay, IKKβ phosphorylation analysis, AKT/p53/p21 Western blot, β-galactosidase and SAHF senescence assays, TRIM22 KO/OE |
Cell death & disease |
High |
38199981
|
| 2024 |
TRIM22 ubiquitinates copper chaperone CCS via K27-linked ubiquitination at CCS Lys76, requiring the TRIM22 coiled-coil domain; CCS degradation suppresses STAT3 phosphorylation by increasing ROS, inhibiting breast cancer proliferation and invasion. |
Label-free proteomics, Co-IP, ubiquitination assay with linkage-specific antibodies, site-directed mutagenesis (K76R of CCS), TRIM22 coiled-coil domain deletion mutant, ChIP-qPCR, ROS measurement, RNA-seq GSEA |
Cancer letters |
High |
39127340
|
| 2024 |
WTAP promotes m6A modification of TRIM22 5'UTR via the m6A reader IGF2BP1, increasing TRIM22 expression; TRIM22 then interacts with OPA1 and induces its ubiquitination, causing mitochondrial dysfunction in diabetic nephropathy. |
RNA immunoprecipitation for m6A detection of TRIM22 5'UTR, Co-IP of TRIM22 with OPA1, ubiquitination assay, mitochondrial function assays |
Redox report |
Medium |
39314036
|
| 2025 |
TRIM22 enhances RIG-I-mediated antiviral signaling by catalyzing K63-linked polyubiquitination of MAVS, activating the TBK1/IRF3 pathway and IFN-β production; TRIM22 also inhibits the MAVS-NLRX1 inhibitory complex assembly. RNA virus infection induces TRIM22 expression via nuclear translocation of transcription factor ELF3, which activates TRIM22 gene transcription. |
Co-IP, K63-specific ubiquitination assay of MAVS, TRIM22 KO/KD with IFN-β reporter and TBK1/IRF3 phosphorylation assay, ELF3 nuclear translocation and ChIP/reporter assay for TRIM22 promoter, MAVS-NLRX1 Co-IP |
Journal of virology |
High |
40162781
|
| 2025 |
TRIM22 functions as a scaffold protein for autophagy initiation: SPRY domain mediates interaction with ATG13 and FIP200; N-terminal region interacts with ULK1 and ATG101; B-box domain is required for interaction with Beclin-1 and assembly of the class III PI3K complex; Beclin-1 and PLEKHM1 compete for overlapping TRIM22 binding regions. This function is independent of E3 ubiquitin ligase activity. |
Co-IP with domain deletion constructs, competitive binding assay, autophagy flux assay (LC3-II, autophagic clearance), TRIM22 KO, mTOR/AMPK activity measurement, primary neuron experiments |
Animal cells and systems |
High |
40337095
|
| 2024 |
TRIM22 ubiquitinates TCF4 via K48-linked ubiquitination mediated by the TRIM22 RING domain, leading to TCF4 proteasomal degradation and suppression of ovarian cancer cell proliferation and invasion. |
Co-IP, ubiquitination assay with RING domain deletion mutant, rescue of TRIM22 phenotype by TCF4 overexpression |
Molecular cancer research |
Medium |
38842601
|
| 2025 |
TRIM22 promotes K63-linked ubiquitination of p21 via its SPRY domain (interaction) and RING domain (catalysis), inducing p21 degradation through the proteasome pathway to accelerate cell cycle progression in melanoma. |
S-protein pulldown of p21 with TRIM22 SPRY domain, ubiquitination assay (K63-linked), CHX chase confirming proteasomal degradation, p21 KD epistasis experiment |
Scientific reports |
Medium |
40593126
|
| 2025 |
TRIM22 ubiquitinates and degrades CDT2 (CRL4 subunit), acting as a novel E3 ligase for CDT2 in HPV-positive cervical cancer cells; E6-mediated p53 degradation downregulates TRIM22 (a p53 target), leading to CDT2 accumulation that promotes cancer cell growth and survival. |
Ubiquitination assay of CDT2 by TRIM22, Western blot and KD/OE for CDT2/TRIM22 relationship, epistasis with E6/E7, p53 transcription of TRIM22 |
Neoplasia |
Medium |
40680432
|
| 2025 |
TRIM22 interacts with KAT2A and promotes its ubiquitination-dependent degradation in melanoma cells; loss of TRIM22 allows KAT2A accumulation, which binds the Notch1 promoter to increase H3K9ac and activate Notch1 transcription, promoting cancer stemness. |
Co-IP, ubiquitination assay, ChIP of KAT2A at Notch1 promoter for H3K9ac, TRIM22 KO/OE, Notch1 inhibitor rescue |
Journal of translational medicine |
Medium |
37415153
|
| 2025 |
HOXC8 transcriptionally activates TRIM22 expression; TRIM22 then ubiquitinates and degrades IκBα, activating NF-κB signaling to drive stemness maintenance in colorectal cancer cells. |
Luciferase reporter and ChIP for HOXC8-TRIM22 promoter interaction, ubiquitination assay of IκBα by TRIM22, NF-κB activity and stemness markers |
Cancer letters |
Medium |
41265630
|
| 2025 |
TRIM22 interacts with ADRB2 (β-2 adrenergic receptor) and negatively regulates ADRB2 expression and JAK2/STAT3 signaling in lung adenocarcinoma cells. |
STRING database prediction, co-immunoprecipitation of TRIM22 with ADRB2, ADRB2 and TRIM22 KD/OE with JAK2/STAT3 Western blot and cell proliferation assay |
Scientific reports |
Low |
40594822
|
| 2021 |
Constitutive TRIM22 expression in lung/respiratory tract epithelia (independent of IFN stimulation) is sufficient to restrict influenza A virus replication by inhibiting viral transcription onset, representing an intrinsic (pre-existing) defense. |
Transcriptomic analysis of human tissues, primary respiratory cell lines, rhesus macaque airway TRIM22 expression, TRIM22 KD with IAV replication assay (viral transcript measurement), comparison of IFN-dependent vs constitutive expression |
Frontiers in cellular and infection microbiology |
Medium |
34621686
|
| 2022 |
TRIM22 negatively regulates MHC class II protein expression through a mechanism other than transcription or protein degradation; TRIM22 KO increases MHC-II protein levels while OE decreases them, without affecting CIITA or MHC-II mRNA levels. |
Cas9-sgRNA knockout and TRIM22 overexpression, Western blot for MHC-II protein and mRNA (qPCR), cycloheximide chase for MHC-II degradation |
Biochimica et biophysica acta. Molecular cell research |
Low |
35777501
|
| 2025 |
TRIM22 promotes GBM cell survival by stabilizing Bcl-2 via non-degradative (non-K48) ubiquitination; TRIM22 binds Bcl-2 and increases its protein expression levels. |
Immunoprecipitation of TRIM22-Bcl-2 complex, ubiquitination microarray, ubiquitination assay, Western blot, flow cytometry apoptosis assay |
Molecular & cellular oncology |
Medium |
40552115
|
| 2024 |
TRIM22 directly interacts with KAT2A and promotes KAT2A ubiquitination and degradation in hepatocellular carcinoma cells, reducing H3K9ac enrichment at the GPX4 promoter and promoting ferroptosis through the KAT2A/GPX4 axis; O-GlcNAcylation of KAT2A at S583 blocks TRIM22-mediated ubiquitination, stabilizing KAT2A. |
Co-IP of TRIM22 with KAT2A, ubiquitination assay, ChIP-qPCR for H3K9ac at GPX4 promoter, ferroptosis markers (Fe2+, MDA, ROS, GSH), O-GlcNAcylation site mutant (S583A), in vivo tumor model |
Histology and histopathology / Cancer science |
Medium |
39698827 42114931
|
| 2025 |
TRIM22 inhibits colorectal cancer metastasis by directly interacting with and ubiquitinating β-Catenin, promoting its degradation and inhibiting EMT; this anti-metastatic effect depends on TRIM22 E3 ligase activity. |
Co-IP of TRIM22 with β-Catenin, ubiquitination assay, TRIM22 OE/KD with β-Catenin rescue, in vivo metastasis model |
Experimental cell research |
Medium |
39978715
|
| 2022 |
TRIM22 negatively regulates TLR3-induced CCL5 expression in human renal proximal tubular epithelial cells; TRIM22 is induced downstream of IFN-β in a TLR3-IFN-β-TRIM22 pathway, and its knockdown upregulates poly(I:C)-induced CCL5 production. |
siRNA knockdown of TRIM22 and IFN-β, poly(I:C) stimulation, TRIM22/CCL5/IFN-β mRNA and protein quantification in hRPTECs |
Molecular biology reports |
Medium |
40080304
|
| 2022 |
TRIM22 directly interacts with Smad2 in gastric cancer cells; overexpression of TRIM22 downregulates Smad2 phosphorylation and Smad3 phosphorylation; Smad2 overexpression reverses TRIM22-induced inhibition of proliferation and migration. |
Co-IP of TRIM22 with Smad2, Western blot for p-Smad2/3, rescue experiment with Smad2 overexpression, in vivo xenograft |
Cell death discovery |
Medium |
34489426
|