Ask about this productRelated genes to: LIMD1 antibody
- Gene:
- LIMD1 NIH gene
- Name:
- LIM domains containing 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1999-01-15
- Date modifiied:
- 2014-11-19
Related products to: LIMD1 antibody
Related articles to: LIMD1 antibody
- The LIM domain protein LIMD1 is a critical regulator of the Hippo signaling pathway, acting to sequester the kinases LATS1/2 to adherens junctions (AJs) in response to mechanical strain. Here, we identify the molecular basis for LIMD1 binding and recruitment of LATS1/2 to AJs. We show that while the LIM domains of LIMD1 are sufficient for AJ localization and binding to LATS1/2, recruitment of LATS1 to AJ requires both the intrinsically disordered region (IDR) in the N-terminus as well as the LIM domains. We further dissected the LIM domains and found that LIM1 and LIM2, but not LIM3, are necessary for LATS1 AJ localization. Point mutations that disrupt strain sensitivity in either the first or second LIM domain disrupt both binding and recruitment of LATS1/2 to AJs. Mechanistically, LIMD1 binds LATS1/2 through a conserved linear motif, the LATS-LATCH, which we identified by AlphaFold modeling and confirmed by biochemical and localization assays. The LATS-LATCH is required for mechanical strain-dependent recruitment of LATS1 and LATS2 to AJs. Further analysis of the LATS2-LATCH showed that it is sufficient for binding to LIMD1 and localization to AJs. Mutation of predicted contact residues within the LATS2-LATCH both disrupts its binding to LIMD1 and localization to AJs. These findings define a bipartite mechanism for LIMD1-dependent recruitment of LATS1/2 involving LIM domain-LATCH interactions and N-terminal IDR functions, providing insight into how mechanical signals are transduced through the Hippo pathway. - Source: PubMed
Publication date: 2026/02/02
De Silva ChamikaKelch Brian AMcCollum Dannel - - Source: PubMed
Publication date: 2026/01/03
Basu MuktaChatterjee AmvrinChakraborty BalarkoChatterjee EsshaGhosh SabnamSamadder SudipPal Dilip KumarRoy AnupChakrabarti JayantaGhosh AmlanPanda Chinmay Kumar - Background & objectivesPersistent infection with high-risk human papillomaviruses (HPV) is a major cause of cervical cancer, inducing the hypoxic response by stabilising hypoxia inducing factor-1 alpha (HIF-1α). Under normoxia, HIF-1α is regulated by tumour suppressors genes, LIMD1 and VHL. This study aimed to elucidate the functional roles of two microRNAs, miR-135b-5p and miR-21-5p, in regulating LIMD1/ VHL and their impact on various cellular phenotypes relevant to progression of cervical cancer. MethodsExpressions of miR-135b-5p, miR-21-5p, LIMD1, and VHL was assessed using quantitative real-time polymerase chain reaction (qRT-PCR). Target validation was performed via dual-luciferase assays. Functional assays (proliferation, migration, invasion, apoptosis, and cell cycle analysis) were conducted in SiHa cells following individual and combined miRNA inhibition. ResultsInhibition of miR-135b-5p and miR-21-5p significantly restored LIMD1 (P=0.019) and VHL (P=0.025), respectively, leading to reduced HIF-1α expression (P<0.03). Dual miRNA inhibition had a profound impact on reducing proliferation, migration, invasion and enhancing apoptosis compared to individual knockdowns, whereas G0/G1 arrest was more profound in individual knockdown compared to control cells. Interpretation & conclusionsmiR-135b-5p and miR-21-5p act synergistically as oncomiRs by suppressing LIMD1 and VHL, promoting HIF-1α-mediated cervical cancer progression. This study demonstrated the synergistic oncogenic role of miR-135b-5p and miR-21-5p in cervical cancer via co-regulation of the LIMD1-VHL-HIF-1α axis. - Source: PubMed
Sultana FarhinChatterjee NilanjanaMukherjee DebicaKumar Panda ChinmayDutta Sankhadeep - Mycoplasma gallisepticum (MG), a leading cause of chronic respiratory disease in poultry, provokes sustained inflammation and immune dysregulation; however, its molecular pathogenesis remains incompletely defined. Here, we identify EZH2-mediated trimethylation of histone H3 lysine 27 (H3K27me3) as a critical host epigenetic modification upregulated during MG infection, both in vitro and in vivo. This repressive histone mark facilitates MG pathogenesis by promoting bacterial adhesion, elevating pro-inflammatory cytokines, and inducing macrophage apoptosis. Pharmacological blockade of EZH2 with GSK343 significantly reduced MG burden, highlighting the pathogenic role of H3K27me3. Integrative transcriptomic and CUT&Tag profiling revealed LIMD1 as a direct epigenetic target silenced by H3K27me3. Functional assays demonstrated that LIMD1 overexpression restores cytokine homeostasis, limits MG replication, and protects against apoptosis, while LIMD1 knockdown reverses these effects. Mechanistically, LIMD1 suppresses Hippo pathway activation, preserving nuclear YAP1 and its downstream anti-inflammatory and pro-survival functions. Notably, LIMD1 was required for the protective effects of EZH2 inhibition, and its function was dependent on intact YAP1 signaling. Collectively, our findings uncover a novel EZH2-H3K27me3-LIMD1-Hippo-YAP1 axis that governs host susceptibility to MG infection. Targeting this epigenetic circuit may offer novel strategies for host-directed therapy against avian mycoplasmosis. - Source: PubMed
Publication date: 2025/11/02
Wang YingjieLi ShiyingGuo QiaoLv ShanZhao WenqingLiu JinQi ZhenpingChen ChunyuKabir Md AhsanulPeng Xiuli - Palmitoylation is implicated in acute kidney injury (AKI) development, but its mechanisms are poorly understood. Our study aimed to identify biomarkers associated with palmitoylation-related genes (PRGs) in AKI and explore their biological mechanisms. We analyzed datasets GSE139061, GSE30718, and GSE174220, identifying intersecting genes through differential expression and WGCNA. Candidate genes were selected via PPI analysis, and biomarkers were identified using machine learning, ROC analysis, and gene expression analysis. A nomogram was constructed, and functional analysis along with Reverse Transcription Quantitative Polymerase Chain Reaction (RT-qPCR) and Western blotting were performed. scRNA-seq analysis was utilized to identify key cell types and their developmental trajectories in AKI. LIMD1 and MBD2 were identified as AKI biomarkers with elevated expression in AKI samples, confirmed by RT-qPCR and Western blotting. A nomogram based on these biomarkers effectively predicted AKI risk. Functional analysis showed co-enrichment in the "valine leucine and isoleucine degradation" pathway. scRNA-seq analysis identified tubular cells as key in AKI pathogenesis, with a developmental trajectory detailed through pseudo-time analysis. LIMD1 and MBD2 were confirmed as AKI biomarkers, with tubular cells identified as crucial in AKI. Our findings provide new insights into AKI treatment strategies. - Source: PubMed
Publication date: 2025/09/29
Sun WeinanWang JuntaoZhang LinaZhang WenwenXu QinShao FengminGu Yue