| 2006 |
LMO7 binds directly to emerin with ~125 nM affinity; the C-terminal half of human LMO7 is sufficient for this interaction in vitro. LMO7 is a nucleocytoplasmic shuttling protein that positively regulates emerin gene transcription (emerin mRNA decreased 93% on LMO7 knockdown), and emerin binding to LMO7 inhibits LMO7 transcriptional activity in a feedback loop. |
In vitro binding assay (affinity measurement), luciferase reporter assay, siRNA knockdown, microarray, real-time PCR |
Human molecular genetics |
High |
17067998
|
| 2004 |
LMO7 is an afadin- and alpha-actinin-binding protein at adherens junctions. It connects the nectin-afadin cell-cell adhesion system to the E-cadherin-catenin system through alpha-actinin, and localizes at cell-cell adherens junctions and apical membranes in epithelial cells. |
Immunoprecipitation, immunofluorescence, immunoelectron microscopy, Western blotting |
The Journal of biological chemistry |
High |
15140894
|
| 2011 |
LMO7 binds the Pax3, MyoD, and Myf5 promoters in C2C12 myoblasts and in vitro, and is required for myoblast differentiation. Emerin competes with these promoters for LMO7 binding, inhibiting LMO7-driven transcriptional activation of MyoD and Pax3 promoters. |
ChIP, in vitro promoter-binding assay, siRNA knockdown, overexpression, Co-IP competition assay |
Journal of cell science |
High |
21525034
|
| 2011 |
LMO7 activates myocardin-related transcription factors (MRTFs) by relieving actin-mediated inhibition in a manner synergistic with Rho GTPase. LMO7 colocalizes with F-actin and reduces the G-actin/F-actin ratio via a Rho-independent mechanism, promoting MRTF-SRF signaling and breast cancer cell migration. |
Reporter assay, siRNA knockdown, G/F-actin fractionation, cell migration assay, colocalization imaging |
Molecular and cellular biology |
High |
21670154
|
| 2013 |
Endogenous LMO7 associates with focal adhesions, co-localizing and co-immunoprecipitating with p130Cas. LMO7 nuclear localization and transcriptional activity increased in p130Cas-null MEFs, indicating that p130Cas-dependent focal adhesion association negatively regulates LMO7 nuclear activity. |
Co-immunoprecipitation, immunofluorescence, genetic knockout (p130Cas-null MEFs), transcriptional reporter assay |
PeerJ |
Medium |
24010014
|
| 2014 |
Lmo7-null mice display growth retardation, decreased muscle fiber size, and impaired skeletal and cardiac function with lower levels of phosphorylated Rb, ERK, and JNK, consistent with altered Rb and MAPK signaling pathways. |
Lmo7-null mouse generation, histological analysis, echocardiography, neuromuscular tests, Western blotting |
Muscle & nerve |
Medium |
24825363
|
| 2019 |
LMO7 is induced by TGF-β in vascular smooth muscle cells and acts as a negative feedback regulator of TGF-β signaling. Mechanistically, the LMO7 LIM domain interacts with AP-1 subunits c-FOS and c-JUN and promotes their ubiquitination and degradation, disrupting AP-1-dependent TGF-β autoinduction. LMO7 deletion amplifies TGF-β signaling, ECM deposition, and neointimal formation. |
SMC-specific and global LMO7 knockout mice, carotid ligation/femoral artery denudation models, knockdown, overexpression, mutagenesis, Co-IP, Western blotting for ubiquitination |
Circulation |
High |
30586711
|
| 2019 |
LMO7 is specifically localized in the cuticular plate and cell junctions of inner ear hair cells. Lmo7 KO mice develop cuticular plate deficiencies (reduced F-actin density, abnormal stereociliar rootlets) and late-onset progressive hearing loss, demonstrating LMO7 is required for cuticular plate integrity and cochlear mechanotransduction. |
Lmo7 KO mouse, immunofluorescence/localization, auditory brainstem response, cochlear mechanics, electron microscopy |
Nature communications |
High |
30850599
|
| 2021 |
The Cryptosporidium rhoptry effector protein ROP1 directly interacts with LMO7 in the host cell terminal web. LMO7 acts as an organizer of epithelial cell polarity and cell-cell adhesion, and genetic ablation of LMO7 in mice impacts parasite burden in vivo. |
Parasite effector screen, direct interaction assay, genetic ablation (LMO7 KO mice), in vivo infection model |
Cell host & microbe |
Medium |
34348092
|
| 2022 |
LMO7 binds non-muscle myosin II (NMII) heavy chain and recruits it to apical junctions and the apical cortex in Xenopus ectoderm. This NMII recruitment is essential for LMO7-mediated apical constriction and promotion of circumferential actomyosin belt formation. LMO7 knockdown decreases NMIIA localization at apical junctions and delays neural tube closure. |
Co-immunoprecipitation, immunofluorescence, morpholino knockdown, overexpression in Xenopus embryos |
Development (Cambridge, England) |
High |
35451459
|
| 2023 |
LMO7 directly degrades PFKFB3 (a glycolysis regulator) through K48-linked polyubiquitination in macrophages. LMO7-mediated PFKFB3 degradation inhibits glycolysis and macrophage activation; PFKFB3 also regulates histone demethylase JMJD3 expression, thereby modulating H3K27me3 levels. This LMO7/PFKFB3/JMJD3 axis modulates macrophage function and inflammatory bowel disease. |
Ubiquitination assay (K48-linkage), Co-IP, siRNA knockdown, Western blotting, murine colitis model |
Acta pharmaceutica Sinica. B |
Medium |
38045056
|
| 2025 |
LMO7 acts as an E3 ubiquitin ligase that binds SMAD7, mediating its polyubiquitination at lysine 70 and proteasomal degradation, thereby increasing the stability of TGF-β receptor 1 (TGFβR1) and promoting profibrotic fibroblast polarization and pulmonary fibrosis. |
Co-IP, ubiquitination assay (site-specific K70 mutation), Western blotting, KO fibroblasts, BLM-induced fibrosis mouse model, AAV-mediated shRNA |
Acta pharmacologica Sinica |
High |
40000880
|
| 2025 |
LMO7 inhibits tumor-associated macrophage (TAM) phagocytosis by promoting K48-linked polyubiquitination at lysine 45 of the β chain of LRP1, leading to its proteasomal degradation. LMO7 deficiency enhances TAM phagocytic activity and antitumor immune responses. |
Ubiquitination assay (K48-linkage, K45 mutation), Co-IP, single-cell RNA-seq, LMO7 KO mouse tumor models, Western blotting |
Advanced science |
High |
41208232
|
| 2026 |
LMO7 acts as an E3 ubiquitin ligase that is recruited to POLR2A (the largest subunit of RNA polymerase II), promoting its ubiquitination and proteasomal degradation. LMO7-mediated POLR2A degradation drives cellular senescence through the MDM4/p53/p21 axis. Depletion of LMO7 abolished POLR2A ubiquitination and reduction in H2O2-induced senescent cells. |
Co-immunoprecipitation, ubiquitination assay, siRNA knockdown, Western blotting, CRISPRa |
Cell death & disease |
Medium |
41896199
|
| 2026 |
LMO7 directly binds MGMT via its F-box domain and promotes K48-linked polyubiquitination and proteasomal degradation of MGMT, increasing temozolomide sensitivity in NSCLC cells. TMZ treatment further strengthens the LMO7-MGMT interaction, creating a positive feedback loop accelerating MGMT degradation. |
Co-IP, ubiquitination assay (K48-linkage), F-box domain mutagenesis, MGMT-C145A catalytic mutant, cell viability assay |
The Journal of biological chemistry |
High |
41763308
|
| 2018 |
A recurrent LMO7-BRAF fusion protein was identified in papillary thyroid carcinoma; enforced expression of LMO7-BRAF stimulated endogenous ERK1/2 phosphorylation and promoted anchorage-independent cell growth, demonstrating oncogenic activity of the fusion. |
RT-PCR, FISH, Sanger sequencing, enforced expression, ERK1/2 phosphorylation assay, anchorage-independent growth assay |
Thyroid |
Medium |
29768105
|
| 2017 |
LMO7 interacts with the spindle assembly checkpoint (SAC) protein MAD1. Overexpression but not depletion of LMO7 caused a SAC defect; the LIM domain of LMO7 interfered with kinetochore localization of MAD2 and BUBR1 but not MAD1. Overexpression of the LIM peptide prolonged mitotic timing and interfered with chromosome congression. |
Co-immunoprecipitation, immunofluorescence, overexpression and knockdown experiments, live-cell imaging of mitosis |
The international journal of biochemistry & cell biology |
Medium |
29158164
|
| 2016 |
LMO7 knockdown in chick primary skeletal muscle cells reduces myotube number and width and reduces MyoD-positive myoblasts. Activation of Wnt/beta-catenin pathway (Wnt3a or Bio treatment) rescues the LMO7 knockdown phenotype, indicating crosstalk between Wnt/beta-catenin and LMO7-mediated signaling in myogenesis. |
siRNA knockdown, immunofluorescence, pharmacological rescue (Wnt3a, Bio) |
FEBS letters |
Medium |
26786059
|
| 2022 |
LMO7 is a positive regulator of fibroblast polarization and intrinsic directed migration (IDM). LMO7 is predominantly incorporated into the cytoskeletons of normal fibroblasts, and its depletion inhibits directed migration on fibronectin-rich surfaces and impairs morphological polarity establishment. |
Cytoskeletal fractionation proteomics, siRNA knockdown, live-cell migration assay, fibronectin-coated surfaces |
Biochemical and biophysical research communications |
Medium |
36442233
|
| 2022 |
LMO7 coordinates with FAK signaling to maintain epithelial junctional integrity under osmotic stress in renal epithelial cells. LMO7 depletion causes junctional integrity loss; FAK inhibition prevents robust cortical F-actin assembly and LMO7 association with cortical F-actin. LMO7-depleted cells show excessive FAK activation, suggesting LMO7 regulates FAK activation. |
siRNA depletion, FAK inhibitor (PF-573228), immunofluorescence, TEER/junctional integrity assay, hypertonic stress model |
Cells |
Medium |
36497072
|
| 2025 |
VILL (villin-like protein) directly interacts with LMO7 (E3 ubiquitin ligase) in the cytoplasm of nasopharyngeal carcinoma cells, as determined by Co-IP and GST pull-down. Overexpression of LMO7 partially counteracted the inhibitory effect of VILL on NPC cell proliferation. |
Co-immunoprecipitation, mass spectrometry, GST pull-down, Western blotting, immunofluorescence, overexpression rescue |
Nan fang yi ke da xue xue bao |
Medium |
40415426
|
| 2026 |
LMO7 ubiquitinates SIRT3, leading to its degradation and subsequent osteoarthritis progression. Molecular experiments confirmed the ability of LMO7 to ubiquitinate SIRT3 in vitro and in vivo. |
Ubiquitination assay, Co-IP, in vitro and in vivo experiments, molecular docking |
BMC biology |
Medium |
41992271
|
| 2026 |
Force-dependent dephosphorylation of Ser355 in the LMO7 myosin-binding domain enhances LMO7 binding to non-muscle myosin II (NMII) and increases NMII abundance at the apical cortex during neural tube closure in Xenopus. LMO7 is required to stabilize actomyosin at the apical cortex at the onset of neural tube folding, suggesting a positive feedback between mechanical forces and LMO7 activity. |
Morpholino knockdown, gain-of-function injection, phospho-specific mutants (Ser355), Co-IP, live imaging in Xenopus embryos |
bioRxivpreprint |
Medium |
41659634
|
| 2005 |
TGF-β1 upregulates LMO7 and a splice variant LMO7S (PDZ domain only) in rat ascites hepatoma cells; LMO7 expression is elevated in highly metastatic clones, and TGF-β1-induced LMO7 upregulation is associated with enhanced invasive capacity. |
Differential hybridization, RT-PCR, invasion assay |
Cancer letters |
Low |
15737692
|