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- W2005570616 abstract "The cyclin-dependant kinase Cdk2 is compartmentalized in endosomes but its role is poorly understood. Here we show that Cdk2 present in hepatic endosome fractions is strictly located in a Triton X-100-resistant environment. The endosomal Cdk2 was found to be associated with the protein tyrosine phosphatase SHP-1, a regulator of insulin clearance, and the actin anchor β-catenin, a known substrate for both Cdk2 and SHP-1. In the plasma membranes and endosome fractions, β-catenin is associated with CEACAM1, also known as regulator of insulin clearance. We show that β-catenin, not CEACAM1, is a substrate for Cdk2. Partial down-modulation of Cdk2 in HEK293 cells increased the rate of insulin internalization. These findings reveal that Cdk2 functions, at least in part, via a Cdk2/SHP-1/β-catenin/CEACAM1 axis, and show for the first time that Cdk2 has the capacity to regulate insulin internalization." @default.
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- W2005570616 date "2011-05-01" @default.
- W2005570616 modified "2023-10-16" @default.
- W2005570616 title "Compartmentalized CDK2 is connected with SHP-1 and β-catenin and regulates insulin internalization" @default.
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- W2005570616 doi "https://doi.org/10.1016/j.cellsig.2011.01.019" @default.
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