AS160 _ TBC1D4
- Known as:
- AS160 _ TBC1D4
- Catalog number:
- Y212667
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- AS160 _ TBC1D4
Related genes to: AS160 _ TBC1D4
- Gene:
- TBC1D4 NIH gene
- Name:
- TBC1 domain family member 4
- Previous symbol:
- -
- Synonyms:
- KIAA0603, AS160, DKFZp779C0666
- Chromosome:
- 13q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-29
- Date modifiied:
- 2015-11-18
Related products to: AS160 _ TBC1D4
Akt substrate of 160 kDa,AS160,AS160,Homo sapiens,Human,KIAA0603,TBC1 domain family member 4,TBC1D4Akt substrate of 160 kDa,AS160,As160,Kiaa0603,Mouse,Mus musculus,TBC1 domain family member 4,Tbc1d4Anti- AS160 TBC1D4 AntibodyAnti-Mouse TBC1D4 (KIAA0603), Rabbit PolyclonalAnti-Mouse TBC1D4 (KIAA0603), Rabbit Polyclonalanti-TBC1D4 (C-Terminus)anti-TBC1D4 (Internal)anti-TBC1D4 (Internal)Anti-TBC1D4 Antibodyanti-TBC1D4, Goat polyclonal to TBC1D4, Isotype IgG, Host GoatAnti-TBC1D4, Rabbit Polyclonal to TBC1D4, Isotype , Host RabbitAntibodies: AS160 _ TBC1D4 HOST: Goat Clonality: pAbAS160 Primary Antibody, TBC1D4, Species: Human Synthetic peptide Source: Rabbit PolyclonalAS160 TBC1D4 Immunizing PeptideAS160 Polyclonal Antibody, Reactivity: H, Gene ID: 9882, Synonyms: TBC1D4 Related articles to: AS160 _ TBC1D4
- - Source: PubMed
Publication date: 2026/07/29
Wu NaJing ZuoqianLv HuinaLiu QunGu MingZhong YifanXing PengMa RuiyangJing Yuchen - AS160 (TBC1D4) is a key regulator of glucose transporter trafficking and is frequently overexpressed in several malignancies. However, the mechanisms regulating its protein stability and its contribution to colon tumor metabolism remain poorly understood. Here, we identify a proteotoxic stress-responsive mechanism regulating AS160 abundance that involves crosstalk between the ubiquitin-proteasome system (UPS), ER stress-related signaling, and autophagy. Paradoxically, proteasome inhibition with MG132 resulted in a dose-dependent reduction of AS160 protein levels in both HCT116 and HT29 colon cancer cells, accompanied by the induction of ER stress markers and autophagy activation, including p62 accumulation and increased LC3-II/LC3-I ratios. In contrast, blockade of lysosomal degradation with chloroquine (CHQ) led to marked AS160 accumulation, suggesting that autophagy drives AS160 turnover under proteotoxic stress. Alleviating ER stress with 4-phenylbutyric acid (4-PBA) or scavenging reactive oxygen species with N-acetylcysteine (NAC) did not prevent AS160 loss following MG132 treatment. Functionally, shRNA-mediated knockdown of AS160 did not significantly alter glucose uptake or total GLUT1 protein levels; however, it increased lactate secretion accompanied by reciprocal changes in lactate transporters including upregulation of the lactate transporter MCT4 and downregulation of MCT1. Overall, our results suggest that the stability of AS160 protein is regulated through autophagy-associated pathways and that reduced AS160 expression is associated with altered lactate handling. Targeting pathways that regulate AS160 stability may therefore represent a strategy to modulate tumor metabolic adaptation. - Source: PubMed
Publication date: 2026/04/24
Reabroi SomrudeeSutjarit NareeratChairoungdua Arthit - Glucose transporter type 4 (GLUT4), encoded by the gene, is the final effector of insulin-stimulated glucose uptake in insulin-sensitive tissues: skeletal muscle, adipose tissue, and cardiac muscle. Its dynamic localization, retained intracellularly under basal conditions and extensively translocated to the plasma membrane upon stimulation, makes it a master regulator of glycemic homeostasis. While the canonical insulin pathway (PI3K/Akt/TBC1D4) is the most potent and specific mechanism in the postprandial state, its dysfunction is centrally associated with insulin resistance and type 2 diabetes mellitus (T2DM). Crucially, robust alternative signaling networks function completely independently of insulin to regulate GLUT4 synthesis and translocation. Prominent among these are contraction-mediated pathways in skeletal muscle, which employ calcium signaling (via CaMKII), mechanical/metabolic stress sensors (via p38 MAPK γ/δ), and AMP-activated protein kinase (AMPK). This review critically integrates current knowledge, linking the molecular architecture and post-translational modifications of GLUT4 to the complex, tissue-specific signaling networks that govern its vesicular trafficking. We emphasize the hierarchy, redundancy, and interdependence of these pathways, highlighting differences between acute translocation and chronic transcriptional adaptations. Finally, we discuss how deciphering insulin-independent mechanisms offers promising therapeutic opportunities, particularly in identifying pharmacological targets that mimic the metabolic benefits of physical exercise. - Source: PubMed
Publication date: 2026/04/13
Ramos-Jiménez ArnulfoRubio-Valles MariazelGuereca-Arvizuo JaimeJuárez-Oropeza Marco ARamos-Hernández Javier AChávez-Guevara Isaac AGonzález-Rodríguez EverardoMoreno-Brito VerónicaHernández Torres Rosa P - Homozygous carriers of a loss-of-function variant in the sucrase-isomaltase (SI) gene (c.273_274delAG) are unable to digest sucrose and parts of starch. The variant is common only in Indigenous Arctic populations such as the Greenlandic Inuit and has been associated with a healthier metabolic profile. In a unique gene-diet intervention, we aimed to study whether the SI genotype modulates the effect of two different diets on glucose homeostasis and lipids. - Source: PubMed
Publication date: 2026/04/17
Senftleber NinnaChristensen Marie Mathilde BCarstensen BendixStæger Frederik FilipFrøst Michael BGillum Matthew PHansen TorbenJørgensen Marit E - Skeletal muscle glucose transporter 4 (GLUT4) translocation to the plasma membrane determines glucose uptake in response to insulin and exercise and is disrupted in insulin resistance, making its experimental measurement critical. Confocal light microscopy is widely used for this purpose because of its ability to provide quantitative, high-resolution spatial information from small tissue amounts. However, conventional immunofluorescence colocalization microscopy lacks sensitivity and specificity in the detection of GLUT4 translocation. We validated the use of exofacial epitope-specific GLUT4 antibodies to quantify sarcolemmal GLUT4 translocation in fixed, nonpermeabilized adult human and rodent muscle fibers. Across human, mouse, and rat muscles, these antibodies sensitively detected stimulus-induced GLUT4 translocation, and labeling was abolished in muscle-specific GLUT4-knockout muscle, confirming specificity. Importantly, this study includes the first unambiguous visualization of endogenous GLUT4 translocation in intact human skeletal muscle fibers after insulin stimulation and exercise. In TBC1D4-knockout rats, insulin-stimulated GLUT4 translocation was absent despite wild-type-level GLUT4 expression, confirming an essential role for TBC1D4 in this process. Thus, exofacial GLUT4 antibodies provide a straightforward, sensitive, and specific approach to quantify endogenous GLUT4 translocation in fixed adult skeletal muscle. - Source: PubMed
Persson Kaspar WFjeldsøe CasperFrandsen Lukas WKnudsen Jonas RKwak SeongEunWang HaiyanVoldstedlund Christian TLeandersson Magnus RWitczak Carol AWojtaszewski Jørgen F PRichter Erik ACartee Gregory DJensen Thomas E