Affinage

LIMD1

LIM domain-containing protein 1 · UniProt Q9UGP4

Length
676 aa
Mass
72.2 kDa
Annotated
2026-06-10
40 papers in source corpus 18 papers cited in narrative 21 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

LIMD1 is a multifunctional LIM-domain scaffold/adaptor protein that integrates tumour-suppressive signaling across hypoxia, transcription, mechanotransduction, and RNA silencing (PMID:22286099, PMID:15542589, PMID:29440237). In the hypoxic response it acts as an enzymatic scaffold that simultaneously binds PHD1/2/3 prolyl hydroxylases and VHL, assembling a PHD-LIMD1-VHL complex that drives HIF-1α hydroxylation and proteasomal degradation; because LIMD1 is itself a HIF-1 transcriptional target, this creates a negative feedback loop that limits HIF-1 output and tumour vascularisation (PMID:22286099, PMID:29930174). In the nucleus LIMD1 interacts with pRB to co-repress E2F-driven transcription, promoting Rb hypophosphorylation, E2F1 downregulation, and G0/G1 arrest (PMID:15542589, PMID:24523249). At cell-cell and cell-matrix contacts LIMD1 functions in Hippo mechanotransduction: its LIM domains bind strained F-actin to localize it to adherens junctions in a tension-dependent manner, and it recruits and inhibits LATS1/2 kinases through a bipartite mechanism combining its N-terminal intrinsically disordered region with a conserved LATS-LATCH motif, thereby controlling YAP1 activity (PMID:29440237, PMID:38426816). The same multivalent IDR and LIM interactions drive force-sensitive liquid-liquid phase separation at focal adhesions to regulate FA maturation, contractility, and durotaxis (PMID:33891898). LIMD1 also serves as a molecular link between the eIF4E-bound mRNA 5' cap and AGO2/miRISC, and is required for productive miRNA-mediated silencing (PMID:20616046). CDK1/JNK-mediated mitotic phosphorylation of LIMD1 is required for proper mitotic progression and its suppression of proliferation, migration, and invasion (PMID:30600590). In mouse models LIMD1 negatively regulates osteoclastogenesis through TRAF6/AP-1 and osteoblast differentiation through canonical Wnt/β-catenin signaling (PMID:17092936, PMID:18657804).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2004 High

    Established the first molecular mechanism for LIMD1 tumour suppression by linking it to the Rb-E2F transcriptional axis, answering how LIMD1 restrains proliferation.

    Evidence Co-IP with pRB, E2F reporter assays, and in vitro/in vivo tumour growth assays

    PMID:15542589

    Open questions at the time
    • Did not define the LIMD1 domain mediating pRB binding
    • Did not establish how nuclear LIMD1 levels are controlled
  2. 2006 High

    Connected LIMD1 to innate immune/bone signaling by showing it potentiates TRAF6-mediated AP-1 activation, defining a cytoplasmic adaptor role distinct from its nuclear function.

    Evidence Co-IP (Limd1-Traf6), AP-1 reporter assays, and Limd1-/- mouse osteoclast precursor phenotyping

    PMID:17092936

    Open questions at the time
    • Mechanism by which LIMD1 enhances TRAF6 signaling not resolved
    • Basal bone homeostasis normal, limiting physiological scope
  3. 2008 Medium

    Demonstrated LIMD1 negatively regulates canonical Wnt/β-catenin signaling in osteoblasts, extending its tumour-suppressive logic to developmental/differentiation control.

    Evidence Limd1-/- calvarial osteoblast and stromal cultures with mineralization assays and nuclear β-catenin staining

    PMID:18657804

    Open questions at the time
    • Direct biochemical link between LIMD1 and Wnt components not shown
    • Single lab, knockout model only
  4. 2010 High

    Revealed an unexpected post-transcriptional role: LIMD1 bridges the eIF4E-capped mRNA 5' end to AGO/miRISC, answering how cap-bound silencing complexes are coupled to miRNA targeting.

    Evidence Reciprocal Co-IPs (Ago1/2, RCK, Dcp2, eIF4E), m7GTP cap pulldown, P-body imaging, and miRNA vs siRNA reporter discrimination

    PMID:20616046

    Open questions at the time
    • Structural basis of the eIF4E/AGO bridging interaction not defined
    • Did not establish transcriptome-wide scope of LIMD1 dependence
  5. 2012 High

    Defined LIMD1 as the scaffold assembling a PHD-LIMD1-VHL complex, explaining how HIF-1α hydroxylation and degradation are spatially organized.

    Evidence Co-IP, pulldown, and siRNA depletion with HIF-1α protein-level and transcriptional reporter readouts in normoxia/hypoxia

    PMID:22286099

    Open questions at the time
    • Did not address how LIMD1 itself is regulated by oxygen
    • Structural arrangement of the ternary complex not determined
  6. 2018 High

    Closed the hypoxia loop by showing LIMD1 is a HIF-1 target gene, establishing a negative feedback circuit limiting HIF output, tumour growth, and vascularisation.

    Evidence Promoter-reporter assays, ChIP, Co-IP, and xenograft growth/vascularisation assays

    PMID:29930174

    Open questions at the time
    • Quantitative dynamics of the feedback loop not modeled
    • Tissue-specificity of the loop not explored
  7. 2011 High

    Identified PU.1 as a major transcriptional activator of LIMD1, beginning to explain how LIMD1 expression is set in specific lineages.

    Evidence Promoter-reporter luciferase with motif mutation, ChIP, EMSA, and PU.1 siRNA knockdown

    PMID:21402070

    Open questions at the time
    • Does not connect PU.1 regulation to a specific functional output of LIMD1
    • Other regulatory inputs not mapped
  8. 2014 Medium

    Mechanistically grounded LIMD1-induced arrest in the Rb-E2F1 axis by showing it drives Rb hypophosphorylation and E2F1 downregulation to block S-phase entry.

    Evidence Bidirectional LIMD1 overexpression/knockdown with Rb phosphorylation immunoblot, BrdU, and cell-cycle FACS in A549 cells

    PMID:24523249

    Open questions at the time
    • Upstream kinase/phosphatase mediating Rb hypophosphorylation not identified
    • Single cell line, single lab
  9. 2016 Medium

    Linked LIMD1 to genome stability by showing it is required for centrosomal localization of BRCA2, suggesting a role in faithful cell division.

    Evidence Yeast two-hybrid, GST pulldown domain mapping, endogenous Co-IP, and shRNA knockdown with centrosome imaging and division analysis

    PMID:27656835

    Open questions at the time
    • Functional consequence for homologous recombination not tested
    • Single lab
  10. 2018 High

    Placed LIMD1 at the core of Hippo mechanotransduction, showing it is specifically required (unlike AJUBA/WTIP) to recruit and inhibit LATS kinases at adherens junctions downstream of Rho/tension.

    Evidence Live-cell imaging, LIMD1 siRNA with LATS localization and YAP1 readouts, Rho activation and density manipulations

    PMID:29440237

    Open questions at the time
    • Molecular contact between LIMD1 and LATS not yet defined at this stage
    • How tension is sensed not resolved here
  11. 2019 High

    Identified CDK1/JNK phosphosites on LIMD1 and showed they are required for mitotic progression and tumour-suppressive function, linking cell-cycle kinases to LIMD1 activity.

    Evidence In vitro kinase assays, phosphosite mutagenesis (4A mutant), mitotic timing, and proliferation/migration/invasion assays in lung cancer cells

    PMID:30600590

    Open questions at the time
    • Which downstream LIMD1 function each phosphosite controls not dissected
    • Phosphatase counter-regulation unknown
  12. 2021 High

    Showed LIMD1 undergoes force-sensitive phase separation at focal adhesions, providing a biophysical mechanism for organizing FA maturation, contractility, and durotaxis.

    Evidence Live imaging, FRAP, phase separation assays, IDR/LIM domain dissection, and stiffness-dependent spreading/migration assays

    PMID:33891898

    Open questions at the time
    • In vivo relevance of condensation not established
    • Relationship between FA condensation and junctional Hippo role not unified
  13. 2024 High

    Defined the LIM domains as the strained-F-actin-binding module necessary and sufficient for tension-dependent junctional localization and LATS1 recruitment, providing the mechanosensing basis for LIMD1 function.

    Evidence Domain truncation and conserved-residue point mutations with actin co-localization and LATS1 recruitment assays under tension manipulation

    PMID:38426816

    Open questions at the time
    • Direct structural demonstration of strained-actin binding not provided
    • Quantitative force thresholds not measured
  14. 2025 Medium

    Resolved the LIMD1-LATS interaction into a bipartite mechanism combining the N-terminal IDR with a conserved LATS-LATCH motif, completing the molecular logic of LATS recruitment.

    Evidence AlphaFold modeling, biochemical binding, point mutagenesis, and LATS1 junctional localization assays (preprint)

    Open questions at the time
    • Preprint, not yet peer-reviewed
    • Structural model not experimentally validated at atomic resolution
  15. 2025 Medium

    Established transcriptome-wide that LIMD1 is required for productive AGO2-miRNA targeting, defining the sequence/thermodynamic features most dependent on LIMD1.

    Evidence Chimeric eCLIP in isogenic LIMD1+/+, +/-, -/- CRISPR cells with mRNA decay and translation repression measurements (preprint)

    Open questions at the time
    • Preprint, not yet peer-reviewed
    • Mechanism by which LIMD1 increases site occupancy not directly resolved
  16. 2025 Medium

    Extended LIMD1 into immune evasion by showing it partners with ARIH1 to ubiquitinate and degrade PD-L1, controlling CD8+ T cell activation.

    Evidence Co-IP (LIMD1-ARIH1), ubiquitination and PD-L1 stability assays in isogenic cells, and CD8+ T cell co-culture (preprint)

    Open questions at the time
    • Preprint, not yet peer-reviewed
    • Whether LIMD1 acts as a substrate adaptor or allosteric activator of ARIH1 not defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How LIMD1's distinct activities — junctional Hippo scaffolding, FA phase separation, nuclear Rb co-repression, cap-miRISC bridging, and ubiquitin-ligase partnering — are coordinated within a single cell remains unresolved.
  • No unified model coupling LIMD1's cytoplasmic, junctional, and nuclear pools
  • Domain-level partitioning of functions not systematically mapped
  • Context determinants selecting among partners unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 3 GO:0003723 RNA binding 2 GO:0008092 cytoskeletal protein binding 2 GO:0140110 transcription regulator activity 2
Localization
GO:0005886 plasma membrane 4 GO:0005634 nucleus 3 GO:0005829 cytosol 2 GO:0005815 microtubule organizing center 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-1640170 Cell Cycle 3 R-HSA-392499 Metabolism of proteins 2 R-HSA-74160 Gene expression (Transcription) 2 R-HSA-8953854 Metabolism of RNA 2 R-HSA-8953897 Cellular responses to stimuli 2 R-HSA-1474244 Extracellular matrix organization 1
Partners
AGO2EGLN1EIF4ELATS1LATS2RB1TRAF6VHL
Complex memberships
PHD-LIMD1-VHL complexadherens junctionmiRISC

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2012 LIMD1 acts as a molecular scaffold that simultaneously binds PHD1/2/3 prolyl hydroxylases and VHL, assembling a PHD-LIMD1-VHL multiprotein complex that creates an enzymatic niche for efficient HIF-1α hydroxylation, ubiquitylation, and proteasomal degradation. Depletion of endogenous LIMD1 increases HIF-1α levels and transcriptional activity; conversely, LIMD1 expression downregulates HIF-1 transcriptional activity in a PHD- and 26S proteasome-dependent manner. Co-immunoprecipitation, pulldown, siRNA depletion with HIF-1α protein level and transcriptional activity readouts Nature cell biology High 22286099
2018 LIMD1 is itself a HIF-1 transcriptional target gene, forming a negative feedback loop: hypoxic induction of LIMD1 increases PHD2-LIMD1-VHL complex formation to promote HIF-1α degradation, thereby limiting HIF-1 target gene expression, tumour growth, and vascularisation. Promoter-reporter assays, ChIP, protein complex analysis (Co-IP), xenograft tumour growth and vascularisation assays EMBO molecular medicine High 29930174
2004 LIMD1 specifically interacts with retinoblastoma protein (pRB), represses E2F-driven transcription, and suppresses expression of genes with E2F1-responsive elements, blocking tumour growth in vitro and in vivo. Co-immunoprecipitation, E2F transcriptional reporter assays, gene expression analysis, in vitro and in vivo tumour growth assays Proceedings of the National Academy of Sciences of the United States of America High 15542589
2018 All three mammalian Ajuba family proteins (AJUBA, LIMD1, WTIP) show tension-dependent localization to adherens junctions; LATS1 and LATS2 show overlapping tension-dependent junctional localization. LIMD1 is specifically required for junctional localization of LATS kinases, and LIMD1 mediates recruitment and inhibition of LATS kinases at junctional complexes downstream of Rho activation to regulate YAP1 and Hippo signaling. Live-cell fluorescence imaging, siRNA knockdown of LIMD1 with LATS localization and YAP1 activity readouts, Rho activation experiments, cell density manipulations Journal of cell science High 29440237
2010 LIMD1 (along with Ajuba and WTIP) localizes to processing bodies (P-bodies), binds Ago1/2, RCK, Dcp2, and eIF4E in vivo, and is required for miRNA-mediated (but not siRNA-mediated) gene silencing. LIMD1 interacts with the mRNA 5' m7GTP cap-protein complex via eIF4E, preventing 4EBP1 and eIF4G interaction, and acts as a molecular link between translationally inhibited eIF4E-m7GTP-5'cap and Ago1/2 within the miRISC complex on the 3'-UTR of mRNA. Co-immunoprecipitation (Ago1/2, RCK, Dcp2, eIF4E), m7GTP cap pulldown, siRNA knockdown with miRNA reporter assays, P-body localization by fluorescence microscopy Proceedings of the National Academy of Sciences of the United States of America High 20616046
2021 LIMD1 undergoes force-sensitive liquid-liquid phase separation (condensation) at focal adhesions (FAs). The multivalent interactions of its intrinsically disordered region (IDR) and LIM domains drive this phase transition, regulated by phosphorylation. Condensed LIMD1 compartments enrich and localize late FA proteins, regulate cell spreading, FA dynamics, cellular contractility, and are critical for durotaxis. Live-cell imaging, FRAP, phase separation assays, phosphorylation analysis, FA protein localization by immunofluorescence, cell spreading/contractility/migration assays on substrates of varying stiffness, IDR and LIM domain truncation/mutation experiments Developmental cell High 33891898
2006 Limd1 interacts with Traf6, a critical cytosolic regulator of RANK-L-regulated osteoclast development, and positively affects Traf6-mediated AP-1 activation. Limd1-/- osteoclast precursor cells are defective in AP-1 activation and NFAT2 induction, and Limd1-/- mice are resistant to physiological and pathologic osteoclastogenic stimuli despite normal basal bone homeostasis. Co-immunoprecipitation (Limd1-Traf6), AP-1 reporter assays, Limd1-/- mouse osteoclast precursor functional assays, NFAT2 expression analysis The Journal of biological chemistry High 17092936
2008 LIMD1 localizes to E-cadherin cell-cell adhesive junctions and also translocates to the nucleus where it functions as an RB co-repressor. In vitro, LIMD1 is phosphorylated during mitosis in HeLa cells and colocalizes with vinculin at focal adhesions. Fluorescence microscopy (colocalization with E-cadherin, vinculin), immunoblotting through cell cycle stages (mitosis detection) Cancer letters Medium 18439753
2019 CDK1 and JNK1/2 phosphorylate LIMD1 at S272, S277, S421, and S424 during mitosis (both drug-induced arrest and normal mitosis). LIMD1 deletion shortens mitotic cell cycle duration; a phosphorylation-deficient mutant LIMD1-4A is less active in suppressing cell proliferation, anchorage-independent growth, cell migration, and invasion in lung cancer cells. In vitro kinase assays (CDK1, JNK1/2 with LIMD1), site-directed mutagenesis (4A mutant), mitotic timing assays, colony formation/migration/invasion assays The FEBS journal High 30600590
2011 PU.1 is a major transcriptional activator of LIMD1. A conserved PU.1-binding motif in the LIMD1 CpG island promoter is required for promoter-driven transcription (mutation reduces transcription by 90%). PU.1 specifically binds the LIMD1 promoter in vivo and siRNA depletion of PU.1 significantly reduces endogenous LIMD1 expression. Promoter-reporter luciferase assays with PU.1 motif mutation, ChIP, EMSA, siRNA knockdown of PU.1 with LIMD1 expression readout FEBS letters High 21402070
2014 LIMD1 induces cell cycle arrest via the Rb-E2F1 axis: ectopic LIMD1 expression in A549 lung cancer cells causes hypophosphorylation of Rb, potentiating Rb function and downregulating E2F1, leading to G0/G1 accumulation and reduced S-phase entry. LIMD1 depletion reverses these effects. Overexpression and siRNA knockdown of LIMD1, immunoblotting for Rb phosphorylation and E2F1, BrdU incorporation, flow cytometry cell cycle analysis Cell biology international Medium 24523249
2016 LIMD1 physically interacts with BRCA2, binding to the conserved region of BRCA2 (amino acids 2750–3094) in vitro. LIMD1 is required for centrosome localization of BRCA2; shRNA-mediated suppression of LIMD1 abolishes centrosomal BRCA2 localization and significantly increases abnormal cell division. Yeast two-hybrid screening, GST pulldown (in vitro binding domain mapping), co-immunoprecipitation (endogenous), shRNA knockdown with immunofluorescence microscopy (centrosome localization) and cell division analysis Oncology research Medium 27656835
2008 Limd1 influences osteoblast progenitor numbers, differentiation, and function. Limd1-/- calvarial osteoblasts display increased mineralization and accelerated differentiation, and Limd1-/- bone marrow stromal cells contain more osteoblast progenitors ex vivo. Increased nuclear β-catenin staining in differentiating Limd1-/- osteoblasts indicates that Limd1 negatively regulates canonical Wnt signaling in osteoblasts. Limd1-/- mouse model, calvarial osteoblast and bone marrow stromal cell cultures, mineralization assays, nuclear β-catenin immunostaining Experimental cell research Medium 18657804
2017 LIMD1 interacts with TRAF6 in EBV-latently infected cells; LIMD1 depletion impairs LMP1 signaling (via IRF4/NFκB), potentiates ionomycin-induced DNA damage and apoptosis, and inhibits p62-mediated selective autophagy. Co-immunoprecipitation (LIMD1-TRAF6), promoter-reporter assays (IRF4/NFκB binding motifs), siRNA depletion with apoptosis and autophagy functional assays Oncotarget Medium 29464072
2020 LIMD1 overexpression in lung adenocarcinoma cells increases GADD45α and p-p38 MAPK levels, increasing cisplatin sensitivity and apoptosis. Pharmacological inhibition of p38 MAPK (SB203580) abolishes the sensitization effect, placing LIMD1 upstream of the GADD45α/p38 MAPK pathway in cisplatin response. Lentiviral overexpression of LIMD1, Western blotting (GADD45α, p38 MAPK), CCK-8 viability, flow cytometry apoptosis, pharmacological p38 inhibition (SB203580) as epistasis test Frontiers in oncology Medium 32754438
2021 SKI interacts with LIMD1 (identified by BioID2 proximity labeling in human cardiac fibroblasts), and LIMD1 is proposed as an intermediary in SKI-mediated Hippo pathway activation to promote LATS2-dependent TAZ proteasomal degradation and inhibit cardiac fibroblast activation. BioID2-based proximity proteomics (mass spectrometry), siRNA knockdown of LATS2 (epistasis), immunoblotting for TAZ/YAP Basic research in cardiology Low 33847835
2024 The LIM domains of LIMD1 (and TRIP6) are necessary and sufficient for tension-dependent localization to adherens junctions. LIMD1 and TRIP6 colocalize with actin fiber ends at adherens junctions, and point mutations in a key conserved residue in each LIM domain (predicted to impair strained f-actin binding) abolish adherens junction localization and the ability to bind and recruit LATS1 to adherens junctions. Fluorescence microscopy (domain truncations and point mutations), co-localization with actin, LATS1 recruitment assays, tension manipulation experiments Cytoskeleton (Hoboken, N.J.) High 38426816
2022 AJUBA and WTIP compete with LIMD1 for association with adherens junctions; overexpression of AJUBA or WTIP reduces junctional localization of both LIMD1 and LATS1, and is associated with increased YAP1 phosphorylation and decreased YAP1 nuclear localization. This indicates LIMD1 is specifically required (unlike AJUBA/WTIP) for recruiting LATS kinases to adherens junctions. Overexpression of AJUBA and WTIP in MCF10A cells with LIMD1 and LATS1 junctional localization assays by fluorescence microscopy, YAP1 phosphorylation and nuclear localization readouts microPublication biology Medium 36439396
2025 LIMD1 binds LATS1/2 through a conserved linear motif called the LATS-LATCH (identified by AlphaFold modeling). LIM1 and LIM2 (but not LIM3) of LIMD1 are necessary for LATS1 adherens junction localization. Recruitment of LATS1 to adherens junctions requires both the N-terminal IDR and the LIM domains of LIMD1. Mutations in the LATS-LATCH disrupt its binding to LIMD1 and its AJ localization, establishing a bipartite mechanism for LIMD1-dependent LATS1/2 recruitment. AlphaFold structural modeling, biochemical binding assays, point mutagenesis, fluorescence localization assays for LATS1 AJ recruitment, domain truncation experiments bioRxivpreprint Medium
2025 LIMD1 is required for productive AGO2-miRNA targeting transcriptome-wide. In LIMD1-deficient human small airway epithelial cells (CRISPR-edited), AGO2-miRNA complexes bind fewer transcripts with lower site occupancy, and both miRNA-mediated mRNA decay and translational repression are reduced. LIMD1 dependence is strongest for GC-poor seed sites, less conserved miRNAs/sites, and thermodynamically stronger duplexes. Chimeric eCLIP in isogenic LIMD1+/+, +/-, and -/- CRISPR-edited human cells, transcriptome-wide AGO2 binding site analysis, mRNA decay and translation repression measurements bioRxivpreprint Medium
2025 LIMD1 interacts with the E3 ubiquitin ligase ARIH1 to mediate PD-L1 ubiquitination and proteasomal degradation. LIMD1 deficiency impairs this process, resulting in increased PD-L1 protein stability and surface expression, leading to suppression of CD8+ T cell activation that is reversible by PD-L1 blockade. Co-immunoprecipitation (LIMD1-ARIH1), ubiquitination assays, PD-L1 stability/degradation assays in isogenic LIMD1-deficient cells, CD8+ T cell activation co-culture functional assays bioRxivpreprint Medium

Source papers

Stage 0 corpus · 40 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2018 Tension-dependent regulation of mammalian Hippo signaling through LIMD1. Journal of cell science 85 29440237
2012 The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity. Nature cell biology 77 22286099
2004 LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded at chromosome 3p21.3, binds pRB and represses E2F-driven transcription. Proceedings of the National Academy of Sciences of the United States of America 70 15542589
2021 LIMD1 phase separation contributes to cellular mechanics and durotaxis by regulating focal adhesion dynamics in response to force. Developmental cell 59 33891898
1999 A novel gene containing LIM domains (LIMD1) is located within the common eliminated region 1 (C3CER1) in 3p21.3. Human genetics 56 10647888
2010 LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing. Proceedings of the National Academy of Sciences of the United States of America 53 20616046
2008 The chromosome 3p21.3-encoded gene, LIMD1, is a critical tumor suppressor involved in human lung cancer development. Proceedings of the National Academy of Sciences of the United States of America 47 19060205
2006 The LIM protein, Limd1, regulates AP-1 activation through an interaction with Traf6 to influence osteoclast development. The Journal of biological chemistry 45 17092936
2021 SKI activates the Hippo pathway via LIMD1 to inhibit cardiac fibroblast activation. Basic research in cardiology 34 33847835
2008 Cell cycle regulated phosphorylation of LIMD1 in cell lines and expression in human breast cancers. Cancer letters 31 18439753
2020 LIMD1-AS1 suppressed non-small cell lung cancer progression through stabilizing LIMD1 mRNA via hnRNP U. Cancer medicine 23 32239804
2023 Super-enhancer-driven lncRNA LIMD1-AS1 activated by CDK7 promotes glioma progression. Cell death & disease 22 37385987
2018 A HIF-LIMD1 negative feedback mechanism mitigates the pro-tumorigenic effects of hypoxia. EMBO molecular medicine 22 29930174
2018 Deregulation of LIMD1-VHL-HIF-1α-VEGF pathway is associated with different stages of cervical cancer. The Biochemical journal 20 29654110
2017 LIMD1 is induced by and required for LMP1 signaling, and protects EBV-transformed cells from DNA damage-induced cell death. Oncotarget 18 29464072
2008 Differential subcellular localisation of the tumour suppressor protein LIMD1 in breast cancer correlates with patient survival. International journal of cancer 16 18712738
2008 The LIM protein LIMD1 influences osteoblast differentiation and function. Experimental cell research 15 18657804
2019 LIMD1 phosphorylation in mitosis is required for mitotic progression and its tumor-suppressing activity. The FEBS journal 13 30600590
2020 miR-550a-5p Functions as a Tumor Promoter by Targeting LIMD1 in Lung Adenocarcinoma. Frontiers in oncology 12 33194664
2014 LIMD1 antagonizes E2F1 activity and cell cycle progression by enhancing Rb function in cancer cells. Cell biology international 11 24523249
2011 PU.1 is a major transcriptional activator of the tumour suppressor gene LIMD1. FEBS letters 11 21402070
2012 Reduced expression of LIMD1 in ulcerative oral epithelium associated with tobacco and areca nut. Asian Pacific journal of cancer prevention : APJCP 9 23167340
2022 PLOD3 regulates the expression of YAP1 to affect the progression of non-small cell lung cancer via the PKCδ/CDK1/LIMD1 signaling pathway. Laboratory investigation; a journal of technical methods and pathology 8 35039611
2021 Algorithm-Based Meta-Analysis Reveals the Mechanistic Interaction of the Tumor Suppressor LIMD1 With Non-Small-Cell Lung Carcinoma. Frontiers in oncology 8 33869018
2020 LIMD1 Increases the Sensitivity of Lung Adenocarcinoma Cells to Cisplatin via the GADD45α/p38 MAPK Signaling Pathway. Frontiers in oncology 7 32754438
2017 Over expression of HIF1α is associated with inactivation of both LimD1 and VHL in renal cell carcinoma: Clinical importance. Pathology, research and practice 7 29033184
2024 The ability of the LIMD1 and TRIP6 LIM domains to bind strained f-actin is critical for their tension dependent localization to adherens junctions and association with the Hippo pathway kinase LATS1. Cytoskeleton (Hoboken, N.J.) 6 38426816
2021 Targeted therapy for LIMD1-deficient non-small cell lung cancer subtypes. Cell death & disease 5 34764236
2018 Differential transmission of the molecular signature of RBSP3, LIMD1 and CDC25A in basal/ parabasal versus spinous of normal epithelium during head and neck tumorigenesis: A mechanistic study. PloS one 5 29672635
2016 Novel BRCA2-Interacting Protein, LIMD1, Is Essential for the Centrosome Localization of BRCA2 in Esophageal Cancer Cell. Oncology research 5 27656835
2025 SMAD3 and p300 complex scaffolding by long non-coding RNA LIMD1-AS1 promotes TGF-β-induced breast cancer cell plasticity. Nucleic acids research 3 40889156
2022 AJUBA and WTIP can compete with LIMD1 for junctional localization and LATS regulation. microPublication biology 3 36439396
2021 Hypomethylation of LIMD1 and P16 by downregulation of DNMT1 results in restriction of liver carcinogenesis by amarogentin treatment. Journal of biosciences 3 34148876
2019 Silencing of LIMD1 promotes proliferation and reverses cell adhesion-mediated drug resistance in non-Hodgkin's lymphoma. Oncology letters 3 30854077
2024 LIMD1-AS1 promotes the progression of prostate cancer and affects the function of prostate cancer cells by down-regulating miR-29c-3p. Journal of cancer research and clinical oncology 2 39636414
2018 Preferential allelic deletion of RBSP3, LIMD1 and CDC25A in head and neck squamous cell carcinoma: Implication in cancer screening and early detection. Cancer biology & therapy 2 29624473
2025 Upregulated LIMD1 alleviates pressure overload-induced cardiac hypertrophy via inhibits YAP1/AKT/GSK3β signaling. PloS one 1 39937832
2015 [Expression and clinical significance of LIMD-1 gene in adult patients with acute leukemia]. Zhongguo shi yan xue ye xue za zhi 1 25687042
2024 Clinical implications of activation of the LIMD1-VHL-HIF1α pathway during head-&-neck squamous cell carcinoma development. The Indian journal of medical research 0 39382421
2023 LncRNA-mir3471-limd1 regulatory network plays critical roles in HIBD. Experimental brain research 0 38147087

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