The Association of ClipR-59 Protein with AS160 Modulates AS160 Protein Phosphorylation and Adipocyte Glut4 Protein Membrane Translocation
| Autor: | Sarwat Cheema, Keyong Du, Wenying Ren |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Scaffold protein
Vesicle-associated membrane protein 8 Biology Biochemistry Mice Adipocytes Animals Humans Protein phosphorylation Phosphorylation Molecular Biology Protein kinase B Glucose Transporter Type 4 Cell Membrane GTPase-Activating Proteins Glucose transporter 3T3 Cells Cell Biology Up-Regulation Cell biology Protein Transport Membrane protein biology.protein Microtubule-Associated Proteins hormones hormone substitutes and hormone antagonists GLUT4 Signal Transduction |
| Zdroj: | Journal of Biological Chemistry. 287:26890-26900 |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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