ArticleMolecular and cellular biology2007
Myosin 5a is an insulin-stimulated Akt2 (protein kinase Bbeta) substrate modulating GLUT4 vesicle translocation.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 113 citations in OpenAlex.
- PIN (Protein Inhibitor of Neuronal Nitric Oxide Synthase) Modulates Glucose Uptake Through NO-Dependent and Independent Mechanisms in Rat Muscle Cells.Antioxidants (Basel, Switzerland) · 2026Article
- GLUT4 Trafficking and Storage Vesicles: Molecular Architecture, Regulatory Networks, and Their Disruption in Insulin Resistance.International journal of molecular sciences · 2025Review
- Cargo adaptors use a handhold mechanism to engage with myosin V for organelle transport.The Journal of cell biology · 2025Article
- Exercise training and cold exposure trigger distinct molecular adaptations to inguinal white adipose tissue.Cell reports · 2024Article
- In-depth urinary and exosome proteome profiling analysis identifies novel biomarkers for diabetic kidney disease.Science China. Life sciences · 2023Article
- MYH10 Governs Adipocyte Function and Adipogenesis through Its Interaction with GLUT4.International journal of molecular sciences · 2022Article
- GLUT4 On the move.The Biochemical journal · 2022Article
- Microtubules in insulin action: what's on the tube?Trends in endocrinology and metabolism: TEM · 2021Review
- Emerging Roles for AKT Isoform Preference in Cancer Progression Pathways.Molecular cancer research : MCR · 2021Review
- Tmod3 Phosphorylation Mediates AMPK-Dependent GLUT4 Plasma Membrane Insertion in Myoblasts.Frontiers in endocrinology · 2021Article
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- Huntingtin-associated protein 1 plays an essential role in the pathogenesis of type 2 diabetes by regulating the translocation of GLUT4 in mouse adipocytes.BMJ open diabetes research & care · 2020Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Mechanisms of Insulin Action and Insulin Resistance.Physiological reviews · 2018Review
- Rab 10-a traffic controller in multiple cellular pathways and locations.Journal of cellular physiology · 2018Review
- Effect of Hyperglycemia on Purinergic and Nitrergic Inhibitory Neuromuscular Transmission in the Antrum of the Stomach: Implications for Fast Gastric Emptying.Frontiers in medicine · 2018Article
- Characterization of the CLASP2 Protein Interaction Network Identifies SOGA1 as a Microtubule-Associated Protein.Molecular & cellular proteomics : MCP · 2017Article
- Systematic Synergy of Glucose and GLP-1 to Stimulate Insulin Secretion Revealed by Quantitative Phosphoproteomics.Scientific reports · 2017Article
- Live-cell single-molecule labeling and analysis of myosin motors with quantum dots.Molecular biology of the cell · 2017Article
- Integrative mRNA-microRNA analyses reveal novel interactions related to insulin sensitivity in human adipose tissue.Physiological genomics · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Phosphatidylinositol 3-kinase activation of Akt signaling is critical to insulin-stimulated glucose transport and GLUT4 translocation. However, the downstream signaling events following Akt activation which mediate glucose transport stimulation remain relatively unknown. Here we identify an Akt consensus phosphorylation motif in the actin-based motor protein myosin 5a and show that insulin stimulation leads to phosphorylation of myosin 5a at serine 1650. This Akt-mediated phosphorylation event enhances the ability of myosin 5a to interact with the actin cytoskeleton. Small interfering RNA-induced inhibition of myosin 5a and expression of dominant-negative myosin 5a attenuate insulin-stimulated glucose transport and GLUT4 translocation. Furthermore, knockdown of Akt2 or expression of dominant-negative Akt (DN-Akt) abolished insulin-stimulated phosphorylation of myosin 5a, inhibited myosin 5a binding to actin, and blocked insulin-stimulated glucose transport. Taken together, these data indicate that myosin 5a is a newly identified direct substrate of Akt2 and, upon insulin stimulation, phosphorylated myosin 5a facilitates anterograde movement of GLUT4 vesicles along actin to the cell surface.
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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.