SGTA Antibody
- Known as:
- SGTA Antibody
- Catalog number:
- XW-8161
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- SGTA Antibody
Related genes to: SGTA Antibody
- Gene:
- SGTA NIH gene
- Name:
- small glutamine rich tetratricopeptide repeat containing alpha
- Previous symbol:
- SGT
- Synonyms:
- -
- Chromosome:
- 19p13
- Locus Type:
- gene with protein product
- Date approved:
- 1998-03-24
- Date modifiied:
- 2016-01-28
Related products to: SGTA Antibody
Related articles to: SGTA Antibody
- Maintenance of endoplasmic reticulum (ER) proteostasis is essential for cellular homeostasis and survival during stress. Beyond canonical quality control pathways, ER-to-cytosol signaling (ERCYS) enables the reflux of ER-resident proteins into the cytosol, where they can acquire noncanonical functions that promote cell survival. However, the mechanisms governing ERCYS and its relationship to ER stress remain poorly understood. Here, we show that ER protein reflux is restricted to a defined stress window and is governed by the ER redox environment. Mild ER stress maximizes protein reflux, whereas severe or reductive stress markedly suppresses this process. Mechanistically, we identify the ER-resident cochaperones DNAJB12 and DNAJB14 as redox-sensitive regulators of ERCYS. Under mild stress, intramolecular disulfide bonds stabilize DNAJB12 and DNAJB14, thereby supporting efficient protein reflux. In contrast, severe or reductive stress increases intracellular glutathione, reducing these disulfide bonds and promoting degradation of DNAJB12 and DNAJB14, resulting in the loss of chaperone-mediated reflux. We further show that protein reflux requires cysteine-dependent interactions between refluxed substrates and the cytosolic cochaperone SGTA, revealing a previously unrecognized redox-sensitive step in the ERCYS pathway. When ERCYS is impaired during severe ER stress, cells instead engage an alternative apoptosis-associated pathway mediated by BAX/BAK-dependent ER membrane permeabilization. This transition is driven by enhanced recruitment of BAX and BAK to the ER by the BH3-only protein BIK, amplifying apoptotic signaling. Together, these findings establish redox regulation as a molecular switch that determines whether cells mount an adaptive ER protein reflux response or commit to BAX/BAK-dependent ER membrane permeabilization and apoptosis. - Source: PubMed
Publication date: 2026/07/25
Abu Madegam LailaGavriel NoaAdebisi Raifu TolulopeIgbaria Aeid - Object detection in sports videos serves as a fundamental task for applications such as intelligent broadcasting, tactical analysis, and athlete tracking. Existing methods face two critical challenges when processing sports scenarios: (1) Motion blur-induced feature degradation, where fast-moving objects generate severe motion blur that leads to indistinct boundaries, texture loss, and significantly reduced feature response intensity, severely weakening the discriminative capability of detectors; (2) Temporal aggregation failure, where existing temporal methods assume small inter-frame displacements that enable effective alignment, yet fast-moving objects often exhibit excessive inter-frame displacement that causes alignment failure, making multi-frame aggregation introduce noise and degrade detection accuracy. To address these challenges, we propose MoSA-Det, a framework whose core idea is to leverage motion states as regulatory signals for detection strategies, achieving joint adaptive optimization of feature extraction and temporal fusion. The framework comprises two core modules: the Motion-Aware Adaptive Feature Module (MAAF) and the State-Guided Temporal Aggregation Module (SGTA). Specifically, MAAF constructs a lightweight motion state estimator through inter-frame feature differencing and local correlation analysis to generate fine-grained motion state priors, and employs a state-conditioned dynamic convolution mechanism to perform weighted fusion of multi-scale receptive field features, introducing deformable convolution for adaptive spatial sampling in high-speed motion regions to effectively alleviate feature degradation caused by motion blur. SGTA embeds motion state priors into the temporal feature fusion process, achieving selective aggregation of inter-frame features through state-aware adaptive weights, ensuring that static regions fully exploit multi-frame information to enhance feature stability while enabling fast-moving regions to avoid noise interference from misaligned frames. Experiments on the SoccerNet-Tracking and SportsMOT datasets demonstrate that MoSA-Det improves [email protected] by 1.7% and 1.6%, and [email protected] by 2.6% and 1.8% over the strongest baselines, respectively, validating the effectiveness of the motion state adaptive strategy. - Source: PubMed
Publication date: 2026/04/03
Yang LuluSun WenqingRen Jinkui - BACKGROUND: Interorganellar protein redistribution is an emerging but underexplored aspect of proteostasis and cellular adaptation. Beyond canonical transcriptional and translational regulation, cells dynamically reprogram the spatial distribution of proteins to rapidly respond to environmental stress. This spatial plasticity enables single gene products to acquire novel, context-dependent functions on the basis of subcellular localization. Such relocalization is particularly pronounced in pathological conditions, such as cancer and viral infections, where proteome remodeling enhances cellular survival and adaptability. We previously defined endoplasmic reticulum (ER)-to-cytosol signaling (ERCYS) as a stress-responsive mechanism that alleviates ER burden by redistributing proteins into the cytosol. Despite growing interest, the molecular mechanisms driving ERCYS and related forms of spatial proteome remodeling remain poorly defined. METHODS: To investigate these mechanisms, we employed siRNA- and CRISPR-based depletion of BIP, SGTA, and DNAJB12/14, coupled with subcellular fractionation and immunoblotting to assess protein localization under stress. Co-immunoprecipitation was used to examine protein–protein interactions, and unfolded protein response (UPR) activation was quantified via quantitative reverse transcription polymerase chain reaction (RT-qPCR). RESULTS: Our results reveal a previously unrecognized role for the UPR in mediating ER protein reflux. Specifically, we show that ATF6 and IRE1, but not PERK, are essential for initiating ERCYS. Notably, IRE1 simultaneously promotes ERCYS while suppressing BAX/BAK-mediated ER membrane permeabilization. Furthermore, we uncover a noncanonical, signaling-independent function of the ER-resident chaperone BIP in protein reflux. BIP forms a complex with membrane-bound DNAJB12/14 and cytosolic SGTA, facilitating chaperone-guided export of proteins from the ER lumen. This process depends on an intact DNAJB12 J-domain and requires BIP to originate within the ER, supporting a directional, regulated export mechanism. These findings challenge the classical view of BIP as solely mediating inward translocation and reveal a bidirectional role in protein trafficking. Our work uncovers a novel layer of UPR-regulated spatial proteome remodeling with potential relevance in cancer biology. - Source: PubMed
Publication date: 2026/02/14
Biadsy SumaGilad AyeletMadegam Laila AbuIgbaria Aeid - Regulation of different metal ions on the properties, structure, self-assembly and encapsulating capabilities of soybean globulin (SG)-tannic acid (TA) conjugates were investigated. Through coordination interactions, metal ions promoted the supramolecular self-assembly of SG, resulting in the efficient encapsulation of β-carotene in its hydrophobic domains. Fe and Cu enhanced particle integrity by forming stable metal-polyphenol networks, while Al and Zn achieved the highest β-carotene encapsulation efficiency due to their appropriate capability to interact with SG/TA and lower destructive effect on β-carotene. In the presence of TA, Fe/Cu imparted strong pH stability to the carriers, Al/Mg/Zn preserved β-carotene under light/heat/oxygen conditions, and Al/Zn promoted superior antioxidant activity and β-carotene bioaccessibility during digestion. These findings demonstrate that metal ions with distinct coordination characteristics significantly influence the functionality of SG-TA conjugates, offering insights for the rational design of metal-induced protein-polyphenol delivery systems. - Source: PubMed
Publication date: 2025/10/17
Xu Qian-DaYu Zhi-LongHe QiangZeng Wei-Cai - Numerous cellular pathways are known to cause resistance in cancer cells. The unfolded protein response (UPR), a signaling pathway activated during proteostasis stress in the endoplasmic reticulum (ER), is an adaptive process to increase cancer cell fitness. However, the molecular mechanism between ER stress, UPR activation, and chemoresistance is insufficiently understood. Here, we report that ER stress induction and UPR activation are necessary for chemoresistance to cisplatin and doxorubicin. Mild ER stress is a sufficient precondition for cancer cells to evade cisplatin- and doxorubicin-associated cell death. Mechanistically, ER stress induction results in the redistribution of PDIA4 from the ER to the cytosol, facilitated by the c-tail-anchored proteins DNAJB12 and DNAJB14 and the cytosolic HSC70-cochaperone SGTA. In the cytosol, PDIA4 forms an inhibitory interaction with caspase-3 and wt-p53, leading to their attenuation and increased cancer cell proliferation. Furthermore, we show that PDIA4 must originate from the ER to inhibit caspase-3 and wt-p53 in the cytosol. Silencing PDIA4, DNAJB12/14, or SGTA rescues wt-p53 and caspase-3 activity. Finally, we found that in tumors isolated from colorectal cancer patients, PDIA4 and DNAJB12 are highly expressed compared to their healthy tissues; this expression is associated with the induction of the UPR. Our data show a novel non-genetic mechanism to inhibit apoptosis and suggest PDIA4, DNAJB12/14, and SGTA as novel therapeutic targets to rescue apoptosis and inhibit proliferation in cancer cells. - Source: PubMed
Publication date: 2025/10/21
Twito GalAbu Abayed Faiza AmteratGilad AyeletBiadsy SumaGavriel NoaSheikh Suliman SuadMizrahi YardenMegged HilaTenenboim MorAbu-Freha NaimIgbaria Aeid