ArticleThe Journal of biological chemistry2012
The association of ClipR-59 protein with AS160 modulates AS160 protein phosphorylation and adipocyte Glut4 protein membrane translocation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Downregulated CLIP3 induces radioresistance by enhancing stemness and glycolytic flux in glioblastoma.Journal of experimental & clinical cancer research : CR · 2021Article
- Current understanding of glucose transporter 4 expression and functional mechanisms.World journal of biological chemistry · 2020Review
- Exercise effects on γ3-AMPK activity, phosphorylation of Akt2 and AS160, and insulin-stimulated glucose uptake in insulin-resistant rat skeletal muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2020Article
- Article
- DHHC7 Palmitoylates Glucose Transporter 4 (Glut4) and Regulates Glut4 Membrane Translocation.The Journal of biological chemistry · 2017Article
- Article
- Elmo2 Is a Regulator of Insulin-dependent Glut4 Membrane Translocation.The Journal of biological chemistry · 2016Article
- The insulin response integrates increased TGF-β signaling through Akt-induced enhancement of cell surface delivery of TGF-β receptors.Science signaling · 2015Article
- Glut4 palmitoylation at Cys223 plays a critical role in Glut4 membrane trafficking.Biochemical and biophysical research communications · 2015Article
- ClipR-59 interacts with Elmo2 and modulates myoblast fusion.The Journal of biological chemistry · 2015Article
- Roles of TBC1D1 and TBC1D4 in insulin- and exercise-stimulated glucose transport of skeletal muscle.Diabetologia · 2015Review
- DHHC17 palmitoylates ClipR-59 and modulates ClipR-59 association with the plasma membrane.Molecular and cellular biology · 2013Article
- Sustained postexercise increases in AS160 Thr642 and Ser588 phosphorylation in skeletal muscle without sustained increases in kinase phosphorylation.Journal of applied physiology (Bethesda, Md. : 1985) · 2012Article
- Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
ClipR-59 is a membrane-associated protein and has been implicated in membrane signaling and vesicle trafficking. Recently, we have identified ClipR-59 as an Akt-interacting protein, and we have found that, by interacting with Akt, ClipR-59 modulates Akt subcellular compartmentalization and Akt substrate AS160 phosphorylation, thereby promoting Glut4 membrane translocation. Here, we have further investigated the regulatory effects of ClipR-59 on AS160 phosphorylation and subsequent adipocyte glucose transport. Our data showed that ClipR-59 interacted with AS160, which was mediated by the ankyrin repeats of ClipR-59 and regulated by insulin signaling. Moreover, the data also demonstrated that the interaction of ClipR-59 with AS160 was required for ClipR-59 to modulate Glut4 membrane translocation as ΔANK-ClipR-59, an AS160 interaction-defective mutant, failed to promote AS160 phosphorylation, Glut4 membrane translocation, and glucose transport induced by insulin in 3T3-L1 adipocytes. Because ClipR-59 also interacts with Akt and enhances the interaction between Akt and AS160, we suggest that ClipR-59 functions as a scaffold protein to facilitate Akt-mediated AS160 phosphorylation, thereby regulating glucose transport.
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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.