ArticleThe Journal of biological chemistry2011
Loss of AS160 Akt substrate causes Glut4 protein to accumulate in compartments that are primed for fusion in basal adipocytes.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
- Does GLUT4 Queue? A Mechanistic Mathematical Model for Insulin Response in Adipocytes.Bulletin of mathematical biology · 2025Article
- The Distance Between: An Algorithmic Approach to Comparing Stochastic Models to Time-Series Data.Bulletin of mathematical biology · 2024Article
- Flow cytometry protocol for GLUT4-myc detection on cell surfaces.Bioscience reports · 2024Article
- Article
- Normalization of maternal adiponectin in obese pregnant mice prevents programming of impaired glucose metabolism in adult offspring.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Article
- GLUT4 On the move.The Biochemical journal · 2022Article
- AKT ISOFORMS-AS160-GLUT4: The defining axis of insulin resistance.Reviews in endocrine & metabolic disorders · 2021Review
- Role of Akt isoforms in neuronal insulin signaling and resistance.Cellular and molecular life sciences : CMLS · 2021Article
- Signaling Heterogeneity is Defined by Pathway Architecture and Intercellular Variability in Protein Expression.iScience · 2021Article
- Current understanding of glucose transporter 4 expression and functional mechanisms.World journal of biological chemistry · 2020Review
- Cadmium exposure enhances organic cation transporter 2 trafficking to the kidney membrane and exacerbates cisplatin nephrotoxicity.Kidney international · 2020Article
- De Novo Lipogenesis as a Source of Second Messengers in Adipocytes.Current diabetes reports · 2019Review
- Thirty sweet years of GLUT4.The Journal of biological chemistry · 2019Review
- A high-throughput chemical-genetics screen in murine adipocytes identifies insulin-regulatory pathways.The Journal of biological chemistry · 2019Article
- Chemical biology probes of mammalian GLUT structure and function.The Biochemical journal · 2018Review
- A systems biology analysis connects insulin receptor signaling with glucose transporter translocation in rat adipocytes.The Journal of biological chemistry · 2017Article
- Antioxidant, Antiglycation, and Hypoglycaemic Effect ofEvidence-based complementary and alternative medicine : eCAM · 2017Article
- AS160 controls eukaryotic cell cycle and proliferation by regulating the CDK inhibitor p21.Cell cycle (Georgetown, Tex.) · 2016Article
- Glut4 Is Sorted from a Rab10 GTPase-independent Constitutive Recycling Pathway into a Highly Insulin-responsive Rab10 GTPase-dependent Sequestration Pathway after Adipocyte Differentiation.The Journal of biological chemistry · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Akt substrate AS160 (TCB1D4) regulates Glut4 exocytosis; shRNA knockdown of AS160 increases surface Glut4 in basal adipocytes. AS160 knockdown is only partially insulin-mimetic; insulin further stimulates Glut4 translocation in these cells. Insulin regulates translocation as follows: 1) by releasing Glut4 from retention in a slowly cycling/noncycling storage pool, increasing the actively cycling Glut4 pool, and 2) by increasing the intrinsic rate constant for exocytosis of the actively cycling pool (k(ex)). Kinetic studies were performed in 3T3-L1 adipocytes to measure the effects of AS160 knockdown on the rate constants of exocytosis (k(ex)), endocytosis (k(en)), and release from retention into the cycling pool. AS160 knockdown released Glut4 into the actively cycling pool without affecting k(ex) or k(en). Insulin increased k(ex) in the knockdown cells, further increasing cell surface Glut4. Inhibition of phosphatidylinositol 3-kinase or Akt affected both k(ex) and release from retention in control cells but only k(ex) in AS160 knockdown cells. Glut4 vesicles accumulate in a primed pre-fusion pool in basal AS160 knockdown cells. Akt regulates the rate of exocytosis of the primed vesicles through an AS160-independent mechanism. Therefore, there is an additional Akt substrate that regulates the fusion of Glut4 vesicles that remain to be identified. Mathematical modeling was used to test the hypothesis that this substrate regulates vesicle priming (release from retention), whereas AS160 regulates the reverse step by stimulating GTP turnover of a Rab protein required for vesicle tethering/docking/fusion. Our analysis indicates that fusion of the primed vesicles with the plasma membrane is an additional non-Akt-dependent insulin-regulated step.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.