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• W1994393417 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." @default.
• W1994393417 created "2016-06-24" @default.
• W1994393417 creator A5008196945 @default.
• W1994393417 creator A5035652016 @default.
• W1994393417 creator A5045019271 @default.
• W1994393417 date "2012-08-01" @default.
• W1994393417 modified "2023-09-30" @default.
• W1994393417 title "The Association of ClipR-59 Protein with AS160 Modulates AS160 Protein Phosphorylation and Adipocyte Glut4 Protein Membrane Translocation" @default.
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• W1994393417 doi "https://doi.org/10.1074/jbc.m112.357699" @default.
• W1994393417 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3411025" @default.
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