Ask about this productRelated genes to: mLST8 antibody
- Gene:
- MLST8 NIH gene
- Name:
- MTOR associated protein, LST8 homolog
- Previous symbol:
- -
- Synonyms:
- Lst8, Pop3, GBL, GbetaL
- Chromosome:
- 16p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2009-05-29
- Date modifiied:
- 2018-06-04
Related products to: mLST8 antibody
Related articles to: mLST8 antibody
- This study aims to enhance milk production and quality in dairy cows. Using cultured MAC-T cells as a model, it seeks to investigate the effects of valine, lysine, and threonine, as well as their optimal combinations, on the synthesis of α-casein by MAC-T cells. Following a 12-h serum starvation period, MAC-T cells were supplemented with varying concentrations of each amino acid individually. The appropriate concentration ranges and optimal levels for valine, lysine, and threonine were determined using ELISA. Response surface methodology was employed to identify the optimal combination of the three amino acids. The resulting α-casein synthesis in the combined treatment group (MIX group) was then compared with that achieved at the individual optimal concentrations and validated by ELISA. Furthermore, mRNA expression levels of the α-casein-encoding gene and key components of the mTOR signaling pathway were analyzed by RT-qPCR, while protein phosphorylation levels were assessed via Western blot. To confirm the functional involvement of the mTOR pathway, a rapamycin-based inhibition assay was conducted. The maximal stimulation of α-casein synthesis in MAC-T cells was observed at valine, lysine, and threonine concentrations of 4 × Val (25.528 mmol/L), 1 × Lys (7.364 mmol/L), and 0.5 × Thr (1.473 mmol/L), respectively. The optimal amino acid combination (MIX) was determined to be valine:lysine:threonine = 36.114:9.027:4.602 mmol/L. α-Casein synthesis in the MIX group was significantly higher than in any individual amino acid supplementation group ( < 0.01). Supplementation with the MIX medium markedly upregulated the relative mRNA expression of α-casein encoding genes ( and ) and key components of the mTOR signaling pathway (, , , , , , , , and ), as well as enhanced the phosphorylation levels of mTOR pathway-related proteins (mTOR, S6K1, 4EBP1, RPS6, and eEF2) ( < 0.01). Treatment with rapamycin significantly suppressed the mRNA expression of these genes, reduced protein phosphorylation, and inhibited α-casein synthesis ( < 0.01); however, co-supplementation with the optimal amino acid combination partially alleviated this suppression, indicating a protective regulatory role of the MIX formulation. The optimal combination of valine, lysine, and threonine was determined to be 36.114:9.027:4.602 mmol/L, corresponding to an approximate molar ratio of 8:2:1. This specific ratio significantly promotes α-casein synthesis in MAC-T cells through activation of the mTOR signaling pathway. - Source: PubMed
Publication date: 2026/03/18
Yang MinZhang XinyuDing YuXie LewenGao YuYao KangyuRen WanpingYang LiangZhao YankunShao Wei - Autophagy dysregulation plays a crucial role in the early pathological stage of Parkinson’s disease (PD), in which dopaminergic (DAergic) neurons undergo degeneration. Transcranial direct current stimulation (tDCS) has shown promising neuroprotective effects in studies related to PD. However, the molecular basis underlying its effects remains unclear, and direct evidence regarding whether it exerts neuroprotective effects through the reactivation of autophagic homeostasis is still lacking. - Source: PubMed
Publication date: 2026/01/03
Tian ZekunLong ChaoWei JuanJiang YanLiu YiLiu ZhenyuLi ManxiaYang KeshuDing ChengbiaoHsieh Tsung-HsunFeng Xiaojun - The mechanistic target of rapamycin complex 2 (mTORC2) signaling pathway, which regulates cell growth and migration, exhibits oncogenic function in colorectal cancer (CRC). mTORC2 signaling is primarily activated by a complex assembly of mTOR, RICTOR, SIN1, and mLST8; however, the mechanisms by which dysregulation of this pathway contributes to its oncogenic function remain elusive. Here, we show that the Src-Like Adaptor Protein (SLAP), a negative regulator of tyrosine kinase signaling receptors, controls mTORC2 integrity to mediate its tumor-suppressive function in CRC. Mechanistically, SLAP interacts with mLST8 and facilitates its non-degradative ubiquitination at lysines 86 and 215, thereby reducing the integrity of mTORC2 and mTORC2-AKT signaling. The E3 ubiquitin ligase UBE3C was identified as a novel SLAP interactor involved in this ubiquitination process. Functionally, SLAP inhibition of CRC cell growth and invasion was dependent upon mTORC2 signaling inhibition. In immunodeficient mice CRC xenografts, SLAP depletion enhanced mTORC2 activity and sensitized CRC cells to mTOR catalytic inhibitors. Together, our findings reveal a previously unrecognized SLAP-UBE3C-mLST8 axis that regulates mTORC2 integrity and suggest a potential therapeutic avenue for targeting mTORC2 in CRC. - Source: PubMed
Publication date: 2025/12/15
Mevizou RudyNaim DanaCauchois FlorentNaudin CécileGreaves GeorgiaEspie KevinFelipe BastienSimon ValérieBoublik YvanNguyen JulieUrbach SergeRoche SergeSirvent Audrey - The aim of this study was to characterize the transcriptional landscape of tuberous sclerosis complex-associated renal angiomyolipomas (TSC-AMLs) using spatial transcriptomics and to compare it with sporadic AMLs and renal cell carcinoma (RCC) to identify TSC-specific molecular features. Spatial gene expression analysis (CytAssist Visium) was performed on formalin-fixed, paraffin-embedded sections from one case each of TSC-AML, sporadic AML, and RCC. Unsupervised clustering revealed that TSC-AML and sporadic AML, unlike RCC, displayed triphasic tumor structures with vascular, smooth muscle, and adipose components expressing canonical perivascular epithelioid cell markers such as PMEL, MLANA, ACTB, and DES. TSC1 and TSC2 were downregulated, and mild upregulation of MTOR, MLST8, and RPTOR was observed, consistent with mTORC1 hyperactivation, whereas RCC showed broader pathway activation. Spatial pathway analysis indicated shared differentiation programs in smooth muscle regions but unique angiogenesis, extracellular matrix remodeling (Wnt and NABA matrisome), and lipid metabolic (PPAR signaling) enrichment in TSC-AML. Comparative profiling identified 42 genes uniquely upregulated in TSC-AML, including GRIA2, FABP4, and IL33, defining candidate TSC-AML-enriched features. Despite the single-case design, this pilot study provides hypothesis-generating insights into TSC-associated renal tumorigenesis and highlights potential biomarkers for future investigation. - Source: PubMed
Publication date: 2025/11/27
Watanabe RyutaFukumoto TetsuyaMiura NoriyoshiKurata MieKitazawa RikoKikugawa TadahikoSaika Takashi - : The mTOR serine/threonine kinase coordinates protein translation, cell growth, and metabolism, and its dysregulation promotes tumorigenesis. We present a reproducible, pan-cancer, network-aware framework that integrates curated resources with genomics to move beyond pathway curation, yielding falsifiable hypotheses and prioritized candidates for mTOR axis biomarker validation. : We assembled -related genes and interactions from GeneCards, KEGG, STRING, UniProt, and PathCards and harmonized identifiers. We formulated a concise working model linking genotype → pathway architecture (mTORC1/2) → expression-level rewiring → phenotype. Three analyses operationalized this model: (i) pan-cancer alteration mapping to separate widely shared drivers from tumor-specific nodes; (ii) expression-based activity scoring to quantify translational/nutrient-sensing modules; and (iii) topology-aware network propagation (personalized PageRank/Random Walk with Restart on a high-confidence STRING graph) to nominate functionally proximal neighbors. Reproducibility was supported by degree-normalized diffusion, predefined statistical thresholds, and sensitivity analyses. : Gene ontology analysis demonstrated significant enrichment for mTOR-related processes (TOR/TORC1 signaling and cellular responses to amino acids). Database synthesis corroborated disease associations involving MTOR and its partners (e.g., , , , , across selected carcinomas). Across cohorts, our framework distinguishes broadly shared upstream drivers (, ) from lineage-enriched nodes (e.g., RICTOR-linked components) and prioritizes non-mutated, network-proximal candidates that align with mTOR activity signatures. : This study delivers a transparent, pan-cancer framework that unifies curated biology, genomics, and network topology to produce testable predictions about the mTOR axis. By distinguishing shared drivers from tumor-specific nodes and elevating non-mutated, topology-inferred candidates, the approach refines biomarker discovery and suggests architecture-aware therapeutic strategies. The analysis is reproducible and extensible, supporting prospective validation of prioritized candidates and the design of correlative studies that align pathway activity with clinical response. - Source: PubMed
Publication date: 2025/10/24
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