Ask about this productRelated genes to: PDLIM2 antibody
- Gene:
- PDLIM2 NIH gene
- Name:
- PDZ and LIM domain 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 8p21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-12-08
- Date modifiied:
- 2016-04-25
Related products to: PDLIM2 antibody
Related articles to: PDLIM2 antibody
- Breast cancer is a life-threatening malignancy with subtle early symptoms, necessitating novel biomarkers and mechanistic insights. The tight junction protein CLDN6 plays a tumor-suppressive role in breast cancer, yet its underlying molecular mechanisms remain incompletely understood. Herein, we demonstrate that CLDN6 suppresses breast cancer growth by inducing autophagic cell death through METTL14-mediated m6A modification of SOX4 mRNA. Mechanistically, CLDN6 sequesters PDLIM2 at the cell membrane, reducing nuclear PDLIM2-mediated RelA ubiquitination. Accumulated RelA transcriptionally upregulates METTL14, enhancing SOX4 mRNA m6A modification and degradation, which attenuates PI3K/Akt signaling and triggers autophagic cell death. Moreover, protein expression analysis in breast cancer tissues and bioinformatics analyses reveal an association between the CLDN6/METTL14/SOX4 axis and patient prognosis. These findings identify the CLDN6/METTL14/SOX4 axis as a promising prognostic signature and potential therapeutic target for breast cancer, highlighting the interplay among tight junction protein, epigenetic modification, and autophagic cell death as a conceptual basis for multi-targeted therapeutic strategies. - Source: PubMed
Publication date: 2026/05/01
Jin QiuLiang YingyingQu HuinanQi DaDong YuanSun MinghaoLiu YafangQuan Chengshi - PDLIM2, a PDZ-LIM domain-containing protein expressed highest in the lung and immune cells, serves as a unique tumor suppressor and immune modulator, mainly by turning off the activation of the master transcription factors NF-κB and STAT3. While its role in cancer is established, the involvement of PDLIM2 in viral infection remains unclear. Here we analyzed public gene expression data of blood leukocytes, bronchoalveolar lavage cells, and lung tissues from uninfected healthy humans and those infected with the respiratory virus severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) or influenza. We found that PDLIM2 expression was repressed by viral infection, and notably, this repression correlated with the severity of infectious diseases. Consistently, the expression level of PDLIM2 was negatively associated with NF-κB and STAT3 activity across a diverse range of cell types, such as macrophages, monocytes, neutrophils, T cells, alveolar type 1 and 2 epithelial cells, airway epithelial cells, and fibroblasts. Accordingly, cells with low PDLIM2 expression exhibited aberrant activation of signaling pathways essential for cellular functions and immune responses. These findings highlight PDLIM2 repression as a common mechanism underlying human viral infectious diseases and suggest PDLIM2 as a potential biomarker and therapeutic target for disease prognosis, prevention, and treatment. - Source: PubMed
Gao FengChen Yongzheng WShapiro Steven DXiao GutianQu Zhaoxia - Ulcerative colitis (UC) involves impaired wound healing processes contributing to sustained immune and microbial interactions that aggravate intestinal injury and may progress to colitis-associated cancer (CAC). Here we investigated whether PDLIM2, a known regulator of both epithelial and immune cell fate, contributes to colitis progression. - Source: PubMed
Publication date: 2026/02/10
Ward StephanieCox Orla TRoggiani SaraCrowley TadghTurroni SilviaMelgar SilviaO'Connor Rosemary - Human and mouse studies have established the unique PDZ-LIM domain-containing protein PDLIM2 as a common tumor suppressor that is especially vital for suppressing the tumorigenesis and therapeutic resistance of lung cancer, the leading cause of cancer-related deaths among both men and women. However, the role of PDLIM2 in tumor metastasis, the predominant cause of cancer morbidity and mortality, is yet to be determined. Here, we report that PDLIM2 repression was positively associated with the metastasis of human lung adenocarcinoma, the major type of non-small cell lung cancer that accounts for more than 40% of all cases of human lung cancer. Interestingly, PDLIM2 repression was also correlated with oncogenic KRAS and/or TP53 mutations, two common drivers of human lung adenocarcinoma that often co-occur. In mice, in comparison to concurrently inducing mutant KRAS expression and TP53 deletion, additional co-ablation of PDLIM2 significantly increased the number and size of lung adenocarcinomas in the lung, and more importantly, the distant metastasis of lung tumor cells. The increased metastasis was accompanied by decreased anti-tumor immunity and increased pro-tumor inflammation. These data demonstrate the role of PDLIM2 in suppressing lung adenocarcinoma metastasis, thereby improving our understanding of this crucial tumor suppressor and lung cancer. They also provide a useful model for studying metastasis and testing new lung cancer treatments . - Source: PubMed
Publication date: 2025/12/07
Gao FengXiao YadongZhang HongqiaoShapiro Steven DQu ZhaoxiaXiao Gutian - Endometrial receptivity occurs during a limited time in the menstrual cycle called the 'window of implantation' (WOI) and is required for successful implantation. Endometrial luminal epithelial cells become adhesive to facilitate embryo attachment and implantation; however, how this occurs is poorly understood. We recently identified that myosin heavy chain 10 (MYH10) was abnormally downregulated in infertile organoid endometrial epithelial cells during the WOI, suggesting a role in receptivity. MYH10 regulates cell polarity, adhesion and migration; however, whether it regulates receptivity is unknown. Our research investigated whether MYH10 regulates endometrial epithelial cell adhesive capacity. MYH10 is localized to all major cellular compartments within the endometrium. Immunostaining intensity was higher in luminal epithelial cells during the WOI compared to the proliferative phase in fertile endometrium. However, MYH10 staining was decreased in infertile endometrium. siRNA knockdown of MYH10 in the Ishikawa cell line significantly decreased cell adhesion to human cytotrophoblast-progenitor spheroids. MYH10 knockdown increased PGR and FOXO1 while decreasing PDLIM2 expression. Proteomics analysis following MYH10 knockdown demonstrated altered production of 57 proteins with functions critical in receptivity, including tight junctions. These results demonstrate that MYH10 alters endometrial epithelial cell adhesive capacity primarily via regulation of the actin cytoskeleton, implying an important role in implantation. - Source: PubMed
Sacco MichaelaDowning PoppySantos Leilani LVarshney SwatiTeh Wan TinnZhou WeiDimitriadis Evdokia