ArticleExperimental cell research2014
Regulation of myosin IIA and filamentous actin during insulin-stimulated glucose uptake in 3T3-L1 adipocytes.
Article in Experimental cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
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- More comprehensive relationship between eGDR and sarcopenia in China: a nationwide cohort study with national representation.Diabetology & metabolic syndrome · 2025Article
- Mechanistic Insight into Serine Flux Regulation through Nanoscale Organization of Glucose and Serine Transporters by Substrate Probe-Based Direct Stochastic Optical Reconstruction Microscopy Imaging.Research (Washington, D.C.) · 2025Article
- Association of triglyceride-glucose index with sarcopenia: NHANES 2011-2014.Frontiers in endocrinology · 2024Article
- Sarcopenia and Chronic Complications of Type 2 Diabetes Mellitus.The review of diabetic studies : RDS · 2022Review
- MYH10 Governs Adipocyte Function and Adipogenesis through Its Interaction with GLUT4.International journal of molecular sciences · 2022Article
- Functional expression of TRPM7 as a CaPhysiological reports · 2019Article
- Article
- On-target action of anti-tropomyosin drugs regulates glucose metabolism.Scientific reports · 2018Article
- Septin 7 reduces nonmuscle myosin IIA activity in the SNAP23 complex and hinders GLUT4 storage vesicle docking and fusion.Experimental cell research · 2017Article
- Rac-mediated actin remodeling and myosin II are involved in KATP channel trafficking in pancreatic β-cells.Experimental & molecular medicine · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Insulin stimulated glucose uptake requires the colocalization of myosin IIA (MyoIIA) and the insulin-responsive glucose transporter 4 (GLUT4) at the plasma membrane for proper GLUT4 fusion. MyoIIA facilitates filamentous actin (F-actin) reorganization in various cell types. In adipocytes F-actin reorganization is required for insulin-stimulated glucose uptake. What is not known is whether MyoIIA interacts with F-actin to regulate insulin-induced GLUT4 fusion at the plasma membrane. To elucidate the relationship between MyoIIA and F-actin, we examined the colocalization of MyoIIA and F-actin at the plasma membrane upon insulin stimulation as well as the regulation of this interaction. Our findings demonstrated that MyoIIA and F-actin colocalized at the site of GLUT4 fusion with the plasma membrane upon insulin stimulation. Furthermore, inhibition of MyoII with blebbistatin impaired F-actin localization at the plasma membrane. Next we examined the regulatory role of calcium in MyoIIA-F-actin colocalization. Reduced calcium or calmodulin levels decreased colocalization of MyoIIA and F-actin at the plasma membrane. While calcium alone can translocate MyoIIA it did not stimulate F-actin accumulation at the plasma membrane. Taken together, we established that while MyoIIA activity is required for F-actin localization at the plasma membrane, it alone is insufficient to localize F-actin to the plasma membrane.
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