ArticleInternational journal of biological macromolecules2017
The carboxy-terminal region of the TBC1D4 (AS160) RabGAP mediates protein homodimerization.
Article in International journal of biological macromolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Structural and functional insights into TBC1D17 highlight the importance of the previously uncharacterized Rab-binding domain.Protein science : a publication of the Protein Society · 2026Article
- TBC1D1 functions as a negative regulator of satellite cells for muscle regeneration.Nature communications · 2025Article
- Transcriptomic and epigenomic signatures of liver metabolism and insulin sensitivity in aging mice.Mechanisms of ageing and development · 2025Article
- Osteoblasts induce glucose-derived ATP perturbations in chondrocytes through noncontact communication.Acta biochimica et biophysica Sinica · 2022Article
- Illumination of the Endogenous Insulin-Regulated TBC1D4 Interactome in Human Skeletal Muscle.Diabetes · 2022Article
- New Classification of Macrophages in Plaques: a Revolution.Current atherosclerosis reports · 2020Review
- Cooperative actions of Tbc1d1 and AS160/Tbc1d4 in GLUT4-trafficking activities.The Journal of biological chemistry · 2019Article
- AKT and AMP-activated protein kinase regulate TBC1D1 through phosphorylation and its interaction with the cytosolic tail of insulin-regulated aminopeptidase IRAP.The Journal of biological chemistry · 2018Article
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
Abstract
TBC1D4 (also known as AS160) is a Rab·GTPase-activating protein (RabGAP) which functions in insulin signaling. TBC1D4 is critical for translocation of glucose transporter 4 (GLUT4), from an inactive, intracellular, vesicle-bound site to the plasma membrane, where it promotes glucose entry into cells. The TBC1D4 protein is structurally subdivided into two N-terminal phosphotyrosine-binding (PTB) domains, a C-terminal catalytic RabGAP domain, and a disordered segment in between containing potential Akt phosphorylation sites. Structural predictions further suggest that a region C-terminal to the RabGAP domain adopts a coiled-coil motif. We show that C-terminal region (CTR) region is largely α-helical and mediates TBC1D4 RabGAP dimerization. RabGAP catalytic activity and thermal stability appear to be independent of CTR-mediated dimerization.
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Registered trials
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