Affinage

PDLIM2

PDZ and LIM domain protein 2 · UniProt Q96JY6

Length
352 aa
Mass
37.5 kDa
Annotated
2026-06-10
47 papers in source corpus 24 papers cited in narrative 24 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PDLIM2 is a PDZ-LIM domain protein that operates at the interface of the cytoskeleton and the nucleus, functioning as a nuclear ubiquitin-ligase system that terminates inflammatory and oncogenic transcription-factor signaling (PMID:17468759, PMID:22155789). In the nucleus, its LIM domain anchors it to the nuclear matrix, where it binds the NF-κB subunit p65/RelA, promotes its polyubiquitination, and sequesters it into intranuclear compartments for proteasomal degradation, thereby switching off NF-κB activity (PMID:17468759, PMID:20838382). PDLIM2 enforces this degradation not by acting alone but as a ubiquitin-ligase enhancer (E5) that stabilizes ROC1 and chaperones the ROC1–SCFβ-TrCP cullin-RING ligase complex onto nuclear RelA (PMID:39080804). The same intranuclear degradation mechanism targets the STAT family: PDLIM2 ubiquitinates STAT3 to restrain TH17 differentiation (PMID:22155789), STAT1 in an osteopontin/PKC-dependent manner (PMID:20889505), and STAT2 to limit interferon signaling and confer antiviral resistance (PMID:31374104). It also degrades transforming proteins, K48-ubiquitinating the HTLV-I Tax oncoprotein to suppress cell transformation (PMID:19131544). Through its PDZ domain PDLIM2 binds the cytoskeletal cross-linkers α-actinin-1/-4 and filamin A and co-localizes at stress fibers, linking it to actin organization, cell adhesion, and directional migration (PMID:15505042, PMID:21814175). Its subcellular partitioning is regulated by differentiation- and adhesion-coupled PKC/ERK-dependent serine phosphorylation, which drives cytoplasmic sequestration and consequent nuclear NF-κB activity (PMID:19052146). By coupling these activities, PDLIM2 acts as a tumor suppressor whose loss—driven by ROS/BACH1-mediated repression or miRNA delivery—promotes constitutive STAT3 and NF-κB activation, immune evasion, chemoresistance, and metabolic reprogramming (PMID:33539325, PMID:31757943, PMID:38880883).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2004 High

    Established PDLIM2's first molecular identity as a cytoskeletal adaptor, defining the PDZ domain as the cytoskeleton-binding module before any nuclear role was known.

    Evidence GST pulldown and gel overlay with purified α-actinin-1/-4 and filamin A, plus confocal co-localization at stress fibers in COS-7 cells

    PMID:15505042

    Open questions at the time
    • Did not address any nuclear or ubiquitin-ligase function
    • Functional consequence of cytoskeletal binding not tested in physiological cells
  2. 2007 High

    Revealed PDLIM2 as a nuclear E3 ligase terminator of NF-κB, answering how nuclear p65 is cleared to resolve inflammation.

    Evidence Reciprocal Co-IP, in vivo p65 ubiquitination assay, and PDLIM2-deficient cells/mice with proinflammatory cytokine readouts

    PMID:17468759

    Open questions at the time
    • Did not identify the cullin-RING machinery PDLIM2 recruits
    • Mechanism of intranuclear compartment targeting unresolved
  3. 2008 Medium

    Showed PDLIM2 localization is dynamically partitioned between nucleus and cytoplasm by signaling, explaining how its NF-κB-suppressive activity is switched off.

    Evidence Subcellular fractionation, kinase inhibitor pharmacology, and phosphatase treatment in THP-1 monocyte/macrophage differentiation with NF-κB reporter

    PMID:19052146

    Open questions at the time
    • Specific phosphorylated residues not mapped here
    • Single cell-line model
  4. 2009 High

    Extended the degradation mechanism to a viral oncoprotein, establishing PDLIM2 as a tumor suppressor that clears HTLV-I Tax.

    Evidence Reciprocal Co-IP, K48-linkage-specific ubiquitination assay, nuclear matrix fractionation, and in vivo transformation/oncogenesis assays

    PMID:19131544

    Open questions at the time
    • E3 cofactors for Tax ubiquitination not defined
    • Did not address endogenous substrates beyond Tax
  5. 2010 High

    Defined the domain logic of PDLIM2 function—LIM/nuclear-matrix anchoring versus PDZ/cytoskeletal binding—and showed PKC-phosphorylation of Ser137 licenses STAT1 ubiquitination downstream of osteopontin.

    Evidence Domain deletion and Tax-binding motif mutagenesis with nuclear fractionation; phospho-mutant/phospho-mimetic constructs plus OPN-knockout mice for STAT1

    PMID:20838382 PMID:20889505

    Open questions at the time
    • Kinase acting directly on Ser137 in vivo not isolated
    • How OPN signaling reaches PDLIM2 not fully traced
  6. 2011 High

    Broadened the substrate repertoire to STAT3 and connected PDLIM2 to actin/podocyte biology and to PDZ-dependent recognition of a pathogen ligand.

    Evidence PDLIM2-deficient mice with TH17/granuloma phenotypes (STAT3); Co-IP/yeast two-hybrid with α-actinin-4 and angiomotin-like-1 in podocytes; crystal structure of the PDZ domain bound to H5N1 NS1 ESEV motif with mutagenesis

    PMID:21625420 PMID:21814175 PMID:22155789

    Open questions at the time
    • Whether NS1 binding alters PDLIM2 enzymatic function untested
    • Podocyte data confidence Medium and single-lab
  7. 2013 Medium

    Linked PDLIM2 to upstream ubiquitin-system regulation (COP9 signalosome) and to its own transcriptional induction by vitamin D, integrating it into migration, polarity, and EMT control.

    Evidence PDLIM2-CSN5 Co-IP with cullin deneddylation assays and knockdown migration/polarity readouts; VDRE reporter, ChIP, and promoter demethylation analysis

    PMID:23584482 PMID:24196835

    Open questions at the time
    • Direct enzymatic relationship between PDLIM2 and CSN deneddylation not reconstituted
    • Both single-lab
  8. 2014 Medium

    Placed PDLIM2 in a β1-integrin–RhoA feedback loop governing epithelial polarity, mechanistically connecting its cytoskeletal role to morphogenesis.

    Evidence shRNA knockdown in 3D MCF10A acini with RhoA GTPase activity assays, FAK/cofilin phosphorylation, and FAK/ROCK inhibitor rescue

    PMID:24863845

    Open questions at the time
    • Whether the effect requires PDLIM2 ligase activity unresolved
    • Single 3D culture system
  9. 2019 High

    Consolidated PDLIM2 as a tumor suppressor coupling NF-κB/STAT3 repression to anti-tumor immunity, added STAT2/antiviral function, and defined cytoplasmic β-catenin association.

    Evidence Conditional/global KO mice with anti-PD-1 and chemotherapy treatments and expression profiling; CRISPR KO with STAT2 ubiquitination and flavivirus assays; fractionation/Co-IP/β-catenin reporter with IGF-1/TGFβ stimulation

    PMID:30885980 PMID:31374104 PMID:31757943

    Open questions at the time
    • Distinction between PDLIM2's nuclear suppressor and cytoplasmic β-catenin-promoting roles not mechanistically reconciled
    • β-catenin association data Medium-confidence single-lab
  10. 2020 Medium

    Identified PDLIM7 heterodimerization and a p62/SQSTM1-mediated proteasome-delivery route as a regulatory layer amplifying PDLIM2-driven p65 degradation.

    Evidence PDLIM7-PDLIM2 Co-IP, K63-linkage-specific ubiquitination of PDLIM2, and double-knockdown epistasis with NF-κB/cytokine readouts

    PMID:32849529

    Open questions at the time
    • E3 producing K63 chains on PDLIM2 not identified
    • Single lab
  11. 2021 High

    Embedded PDLIM2 loss in disease-relevant axes (ROS/BACH1 repression driving STAT3-dependent macrophage reprogramming), defined its requirement for M2 polarization, identified TRIM27 as a substrate, and implicated it in microbial transcytosis.

    Evidence Conditional KO mice with BACH1 ChIP and AM phenotyping; KO macrophages with M1/M2 polarization and migration assays; PDLIM2-TRIM27 Co-IP with K27-ubiquitination; BioID2 proximity proteomics with MPRIP validation in endothelial transcytosis

    PMID:33539325 PMID:34228504 PMID:36531051 PMID:41340074

    Open questions at the time
    • TRIM27 and transcytosis findings are Medium-confidence single-lab
    • How the BioID2 interactome connects to ligase activity largely unmapped
  12. 2022 Medium

    Expanded the substrate set into metabolism, showing PDLIM2 ubiquitinates the glycolytic enzyme PFKL and that tumor-derived exosomal miR-222-3p suppresses PDLIM2 to enhance glycolysis.

    Evidence PDLIM2-PFKL ubiquitination assay, Seahorse metabolic assay, miRNA luciferase reporter, and xenograft in LSCC

    PMID:35723199

    Open questions at the time
    • Whether PFKL ubiquitination occurs in the nucleus or cytoplasm unclear
    • Single lab
  13. 2024 Medium

    Resolved the cullin-RING machinery PDLIM2 employs (E5 enhancer of ROC1-SCFβ-TrCP), connected PDLIM2 loss to mitochondrial/oncometabolite/HIF-1α reprogramming, and added circPTPN12 as a PDZ-binding stabilizer.

    Evidence Co-IP and epistatic RNAi of ROC1/Cullin1/β-TrCP with RelA ubiquitination assays; Seahorse, LC-MS oncometabolites, and Lewis lung carcinoma model with HIF-1α inhibitor; RIP/pulldown/ubiquitination for circPTPN12-OTUD6B

    PMID:38880883 PMID:38992675 PMID:39080804

    Open questions at the time
    • circPTPN12 finding is Low-confidence and focused on the circRNA
    • Structural basis of ROC1-SCFβ-TrCP chaperoning not determined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a single protein reconciles cytoplasmic cytoskeletal/β-catenin-promoting roles with nuclear tumor-suppressive ubiquitin ligase activity, and how phosphorylation-driven trafficking dictates which program dominates, remains unresolved.
  • No structure of the full-length protein engaged with its cullin-RING partners
  • Direct kinases controlling localization not definitively identified
  • Substrate selection rules across NF-κB/STAT/Tax/PFKL/TRIM27 not unified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 7 GO:0016874 ligase activity 3 GO:0008092 cytoskeletal protein binding 2 GO:0060090 molecular adaptor activity 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0005634 nucleus 4 GO:0000228 nuclear chromosome 2 GO:0005829 cytosol 2 GO:0005856 cytoskeleton 2
Pathway
R-HSA-168256 Immune System 6 R-HSA-1643685 Disease 5 R-HSA-392499 Metabolism of proteins 5 R-HSA-162582 Signal Transduction 3
Partners
ACTN4CSN5CTNNB1FLNAPDLIM7RELAROC1TRIM27
Complex memberships
PDLIM2-PDLIM7 heterodimerROC1-SCFβ-TrCP ubiquitin ligase complex

Evidence

Reading pass · 24 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2007 PDLIM2 acts as a nuclear ubiquitin E3 ligase that binds the p65 subunit of NF-κB, promotes p65 polyubiquitination, and targets p65 to discrete intranuclear compartments for proteasomal degradation, thereby terminating NF-κB activation. PDLIM2 deficiency results in larger amounts of nuclear p65, defective p65 ubiquitination, and augmented proinflammatory cytokine production. Co-immunoprecipitation, ubiquitination assay, PDLIM2-deficient cells/mice with cytokine readout, nuclear localization imaging Nature immunology High 17468759
2004 PDLIM2 directly interacts with α-actinin-1, α-actinin-4, and filamin A (confirmed by pulldown with purified proteins and gel overlay assay), and co-localizes with α-actinins at stress fibers. The PDZ domain mediates cytoskeletal binding. Co-immunoprecipitation, GST pulldown, gel overlay assay with purified proteins, confocal microscopy in transfected COS-7 cells Investigative ophthalmology & visual science High 15505042
2009 PDLIM2 directly binds the HTLV-I Tax oncoprotein, promotes K48-linked polyubiquitination of Tax, and recruits Tax from its functional sites into the nuclear matrix for proteasomal degradation, thereby suppressing Tax-mediated cell transformation and oncogenesis. Co-immunoprecipitation, ubiquitination assay, nuclear matrix fractionation, in vitro and in vivo transformation/oncogenesis assays Blood High 19131544
2011 PDLIM2 acts as a nuclear ubiquitin E3 ligase targeting STAT3 for polyubiquitination and proteasomal degradation, thereby inhibiting TH17 cell development. PDLIM2 deficiency leads to nuclear STAT3 accumulation, enhanced TH17 differentiation, and exacerbated granuloma formation. Ubiquitination assay, PDLIM2-deficient mice, T-cell differentiation assays, nuclear fractionation Science signaling High 22155789
2010 PDLIM2 binds Tax directly via a putative α-helix motif at amino acids 236–254; selective disruption of this motif abolishes Tax shuttling to the nuclear matrix and ubiquitination-mediated degradation. The C-terminal LIM domain is required for PDLIM2 interaction with the nuclear matrix and for Tax repression, while the N-terminal PDZ domain is dispensable for Tax regulation but mediates cytoskeletal binding. Domain deletion/mutation analysis, co-immunoprecipitation, nuclear matrix fractionation, ubiquitination assay Oncogene High 20838382
2010 PDLIM2 ubiquitinates STAT1 in an osteopontin (OPN)- and protein kinase C-dependent manner. Serine 137 of PDLIM2 is a PKC phosphorylation site required for STAT1 ubiquitination; phospho-mimetic constructs confirm this role. OPN expression is required for PDLIM2 serine phosphorylation and STAT1 ubiquitination in macrophages. In vivo and in vitro ubiquitination assays, phospho-mutant/phospho-mimetic constructs, ChIP assay, OPN-knockout mice The Journal of biological chemistry High 20889505
2011 PDLIM2 acts as an actin-regulating protein in podocyte foot processes, stabilizes stress fibers, and interacts with the actin-associated proteins α-actinin-4 and angiomotin-like-1 as shown by co-immunoprecipitation and yeast two-hybrid analysis. Co-immunoprecipitation, yeast two-hybrid, immunofluorescence, immunoelectron microscopy Kidney international Medium 21814175
2011 The PDZ domain of PDLIM2 selectively binds the ESEV PDZ-binding motif (PBM) of highly pathogenic avian influenza H5N1 NS1, but not the RSEV PBM of human H1N1 NS1. A crystal structure of the PDLIM2 PDZ domain fused with the C-terminal hexapeptide of HN12-NS1 reveals that residues Arg16 and Lys31 of PDLIM2 are critical for this interaction. Yeast two-hybrid, GST pulldown, mammalian two-hybrid, bimolecular fluorescence complementation, X-ray crystallography, PDZ domain mutagenesis PloS one High 21625420
2008 PDLIM2 subcellular localization is regulated by differentiation state: in non-differentiated monocytic THP-1 cells PDLIM2 is predominantly nuclear, whereas PMA-induced differentiation into macrophages shifts PDLIM2 predominantly to the cytoplasm. This cytoplasmic sequestration is associated with cell adhesion and increased nuclear NF-κB activity. The cytoplasmic shift involves PKC/ERK-dependent serine phosphorylation of PDLIM2. Subcellular fractionation, immunofluorescence, phosphatase treatment, kinase inhibitors, PDLIM2 knockdown/overexpression with NF-κB reporter and adhesion assays Journal of leukocyte biology Medium 19052146
2013 PDLIM2 associates with CSN5 (a subunit of the COP9 signalosome) and controls the nuclear accumulation and deneddylation activity of the CSN toward cullin 1 and cullin 3 subunits of cullin-RING ubiquitin ligases. PDLIM2 suppression causes loss of directional migration, inability to polarize the cytoskeleton, and reversal of the EMT phenotype, along with altered activity of β-catenin, AP-1, NFκB, IRFs, STATs, JUN, and p53. Co-immunoprecipitation (PDLIM2-CSN5), deneddylation activity assay, PDLIM2 knockdown with migration/polarity/transcription factor activity readouts Molecular biology of the cell Medium 24196835
2013 PDLIM2 is a direct transcriptional target of 1,25(OH)2D3/VDR signaling; a functional vitamin D response element (VDRE) was identified in the PDLIM2 promoter. 1,25(OH)2D3-induced demethylation of the PDLIM2 promoter enhances its transcription. PDLIM2 is required for vitamin D-induced cell adhesion and for mediating vitamin D suppression of cancer cell migration and invasion. VDRE reporter assay, ChIP, demethylation analysis, PDLIM2 knockdown with adhesion/migration/invasion readouts Oncogene Medium 23584482
2014 PDLIM2 is required for feedback regulation of the β1-integrin–RhoA signaling axis in 3D breast epithelial acini. PDLIM2 suppression increases β1-integrin, IGF-1R, and RACK1 levels, enhances FAK and cofilin phosphorylation and RhoA-GTPase activity, and disrupts cell polarization and acini formation. Inhibition of FAK or ROCK rescues the polarity defect caused by PDLIM2 suppression. shRNA knockdown in 3D MCF10A cultures, RhoA GTPase activity assay, FAK/cofilin phosphorylation Western blot, FAK/ROCK inhibitor rescue Neoplasia (New York, N.Y.) Medium 24863845
2019 PDLIM2 acts as an E3 ubiquitin ligase that promotes nuclear proteasome-dependent degradation of STAT2 (but not STAT1). Interferon-dependent relocalization of STAT1/2 to the nucleus leads to PDLIM2 ubiquitination of STAT2. CRISPR/Cas9 knockout of PDLIM2 increases STAT2 levels after IFNα treatment, retains STAT2 in the nucleus of HCV-infected cells, and increases resistance to several flaviviruses. CRISPR/Cas9 knockout, ubiquitination assay, nuclear fractionation, IFN response assay, flavivirus infection assay PLoS pathogens High 31374104
2020 PDLIM7 heterodimerizes with PDLIM2 to promote synergistic PDLIM2-mediated degradation of p65. Mechanistically, PDLIM7 promotes K63-linked ubiquitination of PDLIM2, and then p62/SQSTM1 binds polyubiquitinated PDLIM2 and the proteasome, facilitating delivery of the NF-κB–PDLIM2 complex to the proteasome for p65 degradation. Co-immunoprecipitation (PDLIM7-PDLIM2 heterodimer), linkage-specific ubiquitination assay, double knockdown with NF-κB/cytokine readouts Frontiers in immunology Medium 32849529
2019 PDLIM2 cytoplasmic retention is controlled by cell adhesion, and nuclear translocation is stimulated by IGF-1 or TGFβ. Cytoplasmic PDLIM2 associates with active β-catenin, and ectopic PDLIM2 expression increases β-catenin levels and its transcriptional activity. Subcellular fractionation, co-immunoprecipitation (PDLIM2–β-catenin), β-catenin reporter assay, IGF-1/TGFβ stimulation Cancer research Medium 30885980
2021 PDLIM2 downregulation in alveolar macrophages is driven by ROS-activated transcription repressor BACH1. PDLIM2 downregulation leads to constitutive STAT3 activation, driving pro-tumorigenic AM polarization, differentiation from attracted monocytes, suppression of CTLs, and decreased AM phagocytosis. This defines a ROS/BACH1/PDLIM2/STAT3 signaling axis. Conditional PDLIM2 KO mice, ROS stimulation, BACH1 ChIP/reporter assay, flow cytometry (AM polarization), phagocytosis assay, CTL suppression assay JCI insight High 33539325
2019 Through nuclear repression of NF-κB/RelA and STAT3, PDLIM2 increases expression of antigen-presentation genes and T-cell activation genes while repressing multidrug resistance genes, rendering cancer cells vulnerable to immune attack and therapies. Global or lung epithelial-specific PDLIM2 deletion in mice causes increased lung cancer development, chemoresistance, and complete resistance to anti-PD-1. Conditional/global KO mice, gene expression profiling, anti-PD-1 treatment, chemotherapy treatment, epigenetic restoration Nature communications High 31757943
2022 PDLIM2 acts as an E3 ubiquitin ligase that ubiquitinates PFKL (phosphofructokinase, liver type), promoting its degradation. In LSCC cells, PDLIM2 inhibits cell proliferation and glycolysis, and M2 macrophage-derived exosomes deliver miR-222-3p to suppress PDLIM2 expression, leading to elevated PFKL and enhanced glycolysis. Ubiquitination assay (PDLIM2–PFKL), Seahorse metabolic assay, miRNA luciferase reporter, PDLIM2 overexpression/knockdown, in vivo xenograft Neoplasma Medium 35723199
2024 PDLIM2 acts as a ubiquitin ligase enhancer (E5) that stabilizes ROC1 (an essential component of SCF ubiquitin ligases) and chaperones the ROC1-SCFβ-TrCP ubiquitin ligase complex to ubiquitinate nuclear NF-κB RelA for proteasomal degradation. Silencing of ROC1, Cullin 1, or β-TrCP blocks RelA ubiquitination and degradation by PDLIM2. Co-immunoprecipitation, RNAi knockdown of ROC1/Cullin1/β-TrCP, ubiquitination assay, nuclear fractionation Cell & bioscience Medium 39080804
2021 PDLIM2 is required for M2 macrophage polarization induced by IL-4, including expression of M2 phenotypic markers, cell adhesion, and cell migration. PDLIM2 is also required for naïve macrophage migration. M1 macrophage activity induced by TLR4, TLR3, or IFNγ was less dependent on PDLIM2. PDLIM2 knockout bone marrow-derived macrophage cultures, M2 polarization assay (IL-4 stimulation), M1 polarization assay, migration assay Frontiers in oncology Medium 36531051
2021 PDLIM2 interacts with TRIM27 and facilitates K27-linked polyubiquitination-mediated proteasomal degradation of TRIM27, thereby attenuating STAT3 signaling. PBXIP1 overexpression in HCC promotes polyubiquitination of PDLIM2 via the ubiquitin-proteasome system, destabilizing PDLIM2. Co-immunoprecipitation (PDLIM2–TRIM27), linkage-specific ubiquitination assay, PBXIP1 overexpression/KD, STAT3 signaling readout European journal of medical research Medium 41340074
2021 PDLIM2 regulates bacterial (E. coli) and fungal (C. neoformans) traversal and exocytosis in brain microvascular endothelial cells. PDLIM2 knockdown specifically impairs microbial transcytosis and egression (but not invasion). Among 210 proximity-biotinylated PDLIM2 interactors identified by BioID2, MPRIP knockdown mimics the PDLIM2 knockdown phenotype, placing MPRIP as a PDLIM2-interacting effector in this process. Calcium ionophore rescues the exocytosis defect. shRNA knockdown, BioID2 proximity labeling, transcytosis/invasion/egression assays, MPRIP knockdown, calcium ionophore rescue Infection and immunity Medium 34228504
2024 PDLIM2 downregulation leads to NF-κB activation, impaired expression of succinate dehydrogenase (SDH) genes, mitochondrial dysfunction, accumulation of succinate and other oncometabolites, buildup of mitochondrial ROS (mtROS), and activation of HIF-1α. HIF-1α inhibition (PX-478) significantly reduces PDLIM2 knockdown-promoted tumor growth in vivo, placing HIF-1α downstream of PDLIM2 loss. Seahorse metabolic assay, LC-MS oncometabolite analysis, flow cytometry (mtROS), DNA microarray, Lewis lung carcinoma mouse model with HIF-1α inhibitor treatment Journal of experimental & clinical cancer research Medium 38880883
2024 CircPTPN12 interacts with the PDZ domain of PDLIM2 and facilitates p65 ubiquitination by PDLIM2. CircPTPN12 also promotes the deubiquitination of PDLIM2 itself by bolstering the PDLIM2/OTUD6B complex, thereby stabilizing PDLIM2. RNA immunoprecipitation, biotin-coupled probe pulldown, FISH, RNA sequencing, ubiquitination assay Molecular cancer Low 38992675

Source papers

Stage 0 corpus · 47 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2007 PDLIM2-mediated termination of transcription factor NF-kappaB activation by intranuclear sequestration and degradation of the p65 subunit. Nature immunology 274 17468759
2004 Pdlim2, a novel PDZ-LIM domain protein, interacts with alpha-actinins and filamin A. Investigative ophthalmology & visual science 83 15505042
2009 PDLIM2 suppresses human T-cell leukemia virus type I Tax-mediated tumorigenesis by targeting Tax into the nuclear matrix for proteasomal degradation. Blood 78 19131544
2011 PDLIM2 inhibits T helper 17 cell development and granulomatous inflammation through degradation of STAT3. Science signaling 77 22155789
2015 Oncovirus Kaposi sarcoma herpesvirus (KSHV) represses tumor suppressor PDLIM2 to persistently activate nuclear factor κB (NF-κB) and STAT3 transcription factors for tumorigenesis and tumor maintenance. The Journal of biological chemistry 57 25681443
2013 PDLIM2 expression is driven by vitamin D and is involved in the pro-adhesion, and anti-migration and -invasion activity of vitamin D. Oncogene 46 23584482
2012 PDLIM2 restricts Th1 and Th17 differentiation and prevents autoimmune disease. Cell & bioscience 44 22731402
2019 Causative role of PDLIM2 epigenetic repression in lung cancer and therapeutic resistance. Nature communications 40 31757943
2010 Molecular determinants of PDLIM2 in suppressing HTLV-I Tax-mediated tumorigenesis. Oncogene 39 20838382
2021 PDLIM2 repression by ROS in alveolar macrophages promotes lung tumorigenesis. JCI insight 37 33539325
2008 Sequestration of PDLIM2 in the cytoplasm of monocytic/macrophage cells is associated with adhesion and increased nuclear activity of NF-kappaB. Journal of leukocyte biology 37 19052146
2017 Klotho ameliorates cyclosporine A-induced nephropathy via PDLIM2/NF-kB p65 signaling pathway. Biochemical and biophysical research communications 34 28315683
2021 PDLIM2: Signaling pathways and functions in cancer suppression and host immunity. Biochimica et biophysica acta. Reviews on cancer 31 34571051
2013 PDLIM2 regulates transcription factor activity in epithelial-to-mesenchymal transition via the COP9 signalosome. Molecular biology of the cell 31 24196835
2024 ESRP1-mediated biogenesis of circPTPN12 inhibits hepatocellular carcinoma progression by PDLIM2/ NF-κB pathway. Molecular cancer 28 38992675
2020 PDLIM7 Synergizes With PDLIM2 and p62/Sqstm1 to Inhibit Inflammatory Signaling by Promoting Degradation of the p65 Subunit of NF-κB. Frontiers in immunology 27 32849529
2011 PDlim2 selectively interacts with the PDZ binding motif of highly pathogenic avian H5N1 influenza A virus NS1. PloS one 23 21625420
2011 Pdlim2 is a novel actin-regulating protein of podocyte foot processes. Kidney international 23 21814175
2019 HCV and flaviviruses hijack cellular mechanisms for nuclear STAT2 degradation: Up-regulation of PDLIM2 suppresses the innate immune response. PLoS pathogens 22 31374104
2017 Global Proteome and Phospho-proteome Analysis of Merlin-deficient Meningioma and Schwannoma Identifies PDLIM2 as a Novel Therapeutic Target. EBioMedicine 22 28126595
2014 Essential function for PDLIM2 in cell polarization in three-dimensional cultures by feedback regulation of the β1-integrin-RhoA signaling axis. Neoplasia (New York, N.Y.) 22 24863845
2019 PDLIM2 Is a Marker of Adhesion and β-Catenin Activity in Triple-Negative Breast Cancer. Cancer research 20 30885980
2017 Exome and transcriptome sequencing identifies loss of PDLIM2 in metastatic colorectal cancers. Cancer management and research 19 29184442
2022 Exosomes from M2 macrophages promoted glycolysis in FaDu cells by inhibiting PDLIM2 expression to stabilize PFKL. Neoplasma 18 35723199
2015 PDLIM2 suppression efficiently reduces tumor growth and invasiveness of human castration-resistant prostate cancer-like cells. The Prostate 18 26499308
2010 Osteopontin and protein kinase C regulate PDLIM2 activation and STAT1 ubiquitination in LPS-treated murine macrophages. The Journal of biological chemistry 18 20889505
2018 Suppression of NF-κB activation by PDLIM2 restrains hepatic lipogenesis and inflammation in high fat diet induced mice. Biochemical and biophysical research communications 16 29852170
2024 Tumor promoting effect of PDLIM2 downregulation involves mitochondrial ROS, oncometabolite accumulations and HIF-1α activation. Journal of experimental & clinical cancer research : CR 15 38880883
2016 Inactivation of the putative ubiquitin-E3 ligase PDLIM2 in classical Hodgkin and anaplastic large cell lymphoma. Leukemia 14 27538486
2021 PDLIM2 prevents the malignant phenotype of hepatocellular carcinoma cells by negatively regulating β-catenin. Cancer gene therapy 10 33398035
2024 PDLIM2 is a novel E5 ubiquitin ligase enhancer that stabilizes ROC1 and recruits the ROC1-SCF ubiquitin ligase to ubiquitinate and degrade NF-κB RelA. Cell & bioscience 8 39080804
2024 The ubiquitination degradation of KLF15 mediated by WSB2 promotes lipogenesis and progression of hepatocellular carcinoma via inhibiting PDLIM2 expression. Journal of gastroenterology and hepatology 7 39638411
2021 PDLIM2 Suppression Inhibit Proliferation and Metastasis in Kidney Cancer. Cancers 7 34203785
2020 PDLIM2 acts as a cancer suppressor gene in non-small cell lung cancer via the down regulation of NF-κB signaling. Molecular and cellular probes 7 32621848
2020 PDLIM2 protects articular chondrocytes from lipopolysaccharide-induced apoptosis, degeneration and inflammatory injury through down-regulation of nuclear factor (NF)-κB signaling. International immunopharmacology 6 32805696
2023 PDLIM2 can inactivate the TGF-β/Smad pathway to inhibit the malignant behavior of ovarian cancer cells. Cell biochemistry and function 5 37170668
2021 Central Nervous System-Infecting Pathogens Escherichia coli and Cryptococcus neoformans Exploit the Host Pdlim2 for Intracellular Traversal and Exocytosis in the Blood-Brain Barrier. Infection and immunity 5 34228504
2025 PDLIM2 Repression: A Common Mechanism in Viral Lung Infection. bioRxiv : the preprint server for biology 4 41000764
2015 [PDLIM2 and Its Role in Oncogenesis--Tumor Suppressor or Oncoprote?]. Klinicka onkologie : casopis Ceske a Slovenske onkologicke spolecnosti 4 26374157
2025 Myeloid PDLIM2 repression as a common mechanism of infection susceptibility in lung diseases. Frontiers in immunology 3 41346604
2022 PDLIM2 is highly expressed in Breast Cancer tumour-associated macrophages and is required for M2 macrophage polarization. Frontiers in oncology 3 36531051
2026 PDLIM2 repression: a common mechanism in viral lung infection. ImmunoHorizons 1 41904702
2025 Beyond structural domains: the emerging roles of PDLIM2 in cellular signaling and cancer progression. Frontiers in physiology 1 40476213
2025 PDLIM2 deficiency mediated by PBXIP1 promotes the proliferation of HCC cells through reducing the polyubiquitination and degradation of TRIM27. European journal of medical research 1 41340074
2025 PDLIM2 in Lung Adenocarcinoma Metastasis. bioRxiv : the preprint server for biology 1 41573961
2011 Construction of a recombinant eukaryotic expression plasmid containing human PDLIM2 gene and its biological activity. Plasmid 1 21784097
2026 Loss of the PDLIM2 protein during chronic colitis promotes inflammation, impaired epithelium recovery, alterations to the microbiome and oxidative stress. Frontiers in endocrinology 0 41743827

Missed literature

Know a paper Affinage missed for PDLIM2? Flag it for the maintainers and the community.

No submissions yet.