Ask about this productRelated genes to: BAG3 Blocking Peptide
- Gene:
- BAG3 NIH gene
- Name:
- BCL2 associated athanogene 3
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 10q26.11
- Locus Type:
- gene with protein product
- Date approved:
- 1999-04-23
- Date modifiied:
- 2019-04-23
Related products to: BAG3 Blocking Peptide
Related articles to: BAG3 Blocking Peptide
- Esophageal squamous cell carcinoma (ESCC) is characterized by immune evasion and poor clinical outcomes. Autophagy has been implicated in tumor-immune interactions, but the molecular factors linking autophagy-associated processes to immune modulation in ESCC remain incompletely defined. We analyzed PSD3 expression in ESCC tissues and its association with prognosis and MHC-I-related molecules. Protein interactions were assessed by co-immunoprecipitation. Autophagy-associated marker changes, autophagic flux, total MHC-I protein levels, and immune cell infiltration were evaluated following PSD3 knockdown in murine and human ESCC models using Western blotting, tandem fluorescent LC3 reporter assays, immunohistochemistry, and single-cell RNA sequencing. Epistasis analysis was performed by silencing ATG7 following PSD3 knockdown. PSD3 was upregulated in ESCC and associated with unfavorable prognosis. PSD3 knockdown was accompanied by changes in autophagy-associated markers and reduced autophagosome abundance. In KYSE150 cells, tandem fluorescent mCherry-eGFP-LC3B analysis showed that PSD3 silencing impaired autophagic flux. PSD3 co-immunoprecipitated with ATG7, BAG3 and TBK1, supporting its association with autophagy-related protein complexes. PSD3 knockdown increased total MHC-I protein levels and was associated with enhanced immune cell infiltration in syngeneic tumor models. Furthermore, ATG7 silencing following PSD3 knockdown selectively restored HLA-E expression, while HLA-ABC and HLA-F showed no clearly distinguishable change. These findings support a working model in which PSD3 is linked to autophagy-associated immune modulation in ESCC. While additional studies are required to define pathway hierarchy and antigen-presentation function more directly, PSD3 emerges as a candidate molecular node for further mechanistic and translational investigation. - Source: PubMed
Publication date: 2026/05/18
Luo ShujuanNurbahati AididarCai BangwuCui HongPeng TianyuanWang WeiLi HuifangChen JiaoLiu QingLu XiaomeiZheng Shutao - Myofibrillar myopathies (MFMs) are a group of protein aggregate diseases characterized by abnormal protein aggregations and myofibrillar disintegration. Myotilinopathy, also named MFM3 or limb-girdle muscular dystrophy type 1A (LGMD1A), is caused by myotilin mutations. Myotilin is degraded by the ubiquitin-proteasome system; however, when this pathway is overloaded under pathophysiological conditions, the protein quality control system leans on the autophagy-lysosome pathway (ALP) to mediate degradation of aggregates. BCL2-associated athanogene 3 (BAG3) protein facilitates aggresome formation and initiates ALP. In this study, we assessed our strategy of reducing the aggregate burden in muscle by overexpressing human BAG3 in TgT57I mice, a model for LGMD1A. Overexpression was achieved by systemic delivery of AAVrh74.tMCK.hBAG3, and outcome measures included functional, histological, and molecular studies. The hBAG3-treated cohort demonstrated increased rotarod duration, treadmill running distance, grip strength, and maximum tetanic response compared to the untreated cohort. Myotilin aggregate burden was significantly decreased, and autophagy levels were normalized in the treated group. As an adaptive response, hBAG3 normalized the endogenous Bag1/Bag3 ratio to that of 3-month-old TgT57I mice. This study provides evidence that our strategy of reducing the aggregate burden in muscle by overexpressing BAG3 may be used as a treatment for protein aggregate myopathies. - Source: PubMed
Publication date: 2026/02/07
Ozes BurcakTong LingyingMoss KyleMyers MorganMorrison LilyeSon EdwardVetter Tatyana ASahenk Zarife - With global cancer cases projected to reach 35 million by 2050 and drug resistance to existing chemotherapeutic drugs remaining a significant threat in cancer therapy, accounting for up to 90% of chemotherapy failures, the search for novel anticancer compounds continues to be increasingly important. This systematic review (2021-2025) examined the role of thiazoles and 4-thiazolidinones/thiazolidinediones as popular scaffolds in existing anticancer drug design. While researchers continue to focus on well-established molecular targets, such as EGFR, VEGFR-2, and tubulin, there is a notable difference regarding other preferred choices for thiazoles and 4-thiazolidinones/thiazolidinediones. Among analyzed mechanisms of anticancer activity notably favored for thiazoles was the inhibition of serine/threonine protein kinases (CDK-2, BRAF), while for 4-thiazolidinones/thiazolidinediones more studied were ROS generation and PPARγ activation. Furthermore, less-researched mechanisms of anticancer activity with no FDA-approved drugs such as PTP1B, SIRT2, PKM2, eIF4E, CA XI and XII inhibition for thiazole derivatives and pan-PIM kinase and BAG3 protein inhibition for 4-thiazolidinones/thiazolidinediones were evaluated as well. Notable was the popularity of the multi-targeting approach for modern drug design, with ~30% reporting two or more targets for their compounds. Despite these advancements, the review identified critical gaps in ADMET evaluations, safety analyzing against normal human cells and the lack of mechanistic studies connecting the targeted protein and the compounds anticancer effects. - Source: PubMed
Publication date: 2026/04/27
Dudchak RostyslavPodolak MagdalenaBielawska AnnaBielawski KrzysztofLesyk Roman - BAG3 (Bcl-2 associated athanogene 3) is a multifunctional protein with pleiotropic effects in multiple cell types. Despite our knowledge of its role in cardiovascular disease, its specific role in endothelial cells (ECs) is unknown. The purpose of this study was to identify differences in the EC proteome of multiple tissues before and after cell specific deletion of Bag3. We hypothesized that BAG3 loss would uniquely alter the baseline proteome landscape of ECs in each tissue. Cdh5(PAC)-CreERT2;Bag3f/f mice received tamoxifen (KO; n=18) or vehicle (WT; n=18) and tissues (brain, heart, lung, and peripheral skeletal muscle-SkM) were collected for FACS of ECs from equal numbers of male and female mice at >22 weeks of age, followed by LC-MS/MS label-free proteomics. Initial comparisons of the WT proteomes between tissues revealed differential abundance of EC proteins (p<0.05), including: 367 brain v heart; 338 brain v lung; 570 brain v SkM; 400 heart v lung; 104 heart v SkM; and 489 lung v SkM. Additionally, the EC mitochondrial proteome was unique to each tissue of origin, with significantly (p<0.05) higher proportions dedicated to complexes I, III, IV and V, in heart compared to the other tissues. KO demonstrated the largest effect on SkM ECs, increasing 31 proteins (Mybpc2 Log2FC=4.81; PFKM Log2FC=3.02) and decreasing 65 (CDC42 Log2FC=-2.44; Prpf8 Log2FC=-2.24). Overall, these results demonstrate that the EC proteome of different tissues is unique and that the loss of BAG3 in these cells differentially alters a small proportion of the EC specific proteome. - Source: PubMed
Publication date: 2026/05/09
Terwilliger Zoë SLi FeifeiPentakota AnanyaZeczycki Tonya NGreen Thomas DKolasa MakenzieEdwards Nancy CGoldman Matthew PFisher-Wellman Kelsey HMcClung Joseph M - Cisplatin resistance remains a major obstacle in the treatment of gastric cancer (GC), and autophagy has been increasingly recognized as a key cytoprotective mechanism contributing to chemoresistance. CREB3L4 is an endoplasmic reticulum membrane-bound transcription factor that has been shown to regulate the expression of Bcl-2 associated athanogene 3 (BAG3), a co-chaperone protein involved in autophagy and survival signaling in various cancers. However, whether the CREB3L4/BAG3 axis regulates autophagy and contributes to cisplatin resistance in gastric cancer cells remains unclear. In the present study, we investigated the roles of CREB3L4 and BAG3 in cisplatin-resistant GC cell lines and found that CREB3L4 and BAG3 were overexpressed. Furthermore, BAG3 expression was inhibited following CREB3L4 knockdown in gastric cancer cells. Notably, knockdown of CREB3L4 inhibited autophagy and alleviated cisplatin resistance in gastric cancer cells by down-regulating BAG3. In addition, silencing of CREB3L4 promoted apoptosis and inhibited cell proliferation, which was also associated with decreased BAG3 expression. Taken together, these findings indicate that depletion of CREB3L4 suppressed autophagy and reduced cisplatin resistance in GC cells by downregulating BAG3. - Source: PubMed
Publication date: 2026/05/07
Yin Wen-KeXie Xue-MeiSong Xiao-YanXiang Yue