Insulin inhibits nuclear phosphatase activity: requirement for the C-terminal domain of the insulin receptor.
Clicks: 112
ID: 272609
1995
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Abstract
Insulin's interaction with its receptor initiates a multitude of cellular effects on metabolism, growth, and differentiation. We recently described an insulin-mediated inhibition of nuclear protein phosphatase 2A (PP-2A), which is associated with an increase in phosphorylation of the transcription factor cAMP response element-binding protein. To clarify the role of nuclear PP-2A inhibition in the insulin signaling cascade, we examined the regulation of this phosphatase activity by insulin in Rat-1 fibroblasts overexpressing normal (HIRc) or mutant human insulin receptors (delta CT cells, deletion of a 43-amino acid C-terminal domain). The delta CT cells represent an excellent model of impaired metabolic and intact mitogenic action of insulin. Insulin inhibited nuclear PP-2A activity and enhanced cAMP response element-binding protein phosphorylation in HIRc cells, but not in delta CT cells. The delta CT cells exhibited normal ras activation and blunted mitogen-activating protein kinase phosphorylation and activation in response to insulin (16-fold in HIRc cells vs. 3-fold in delta CT cells), indicating that the mitogen-activating protein kinase pathway is important for the regulation of nuclear PP-2A activity by insulin. We conclude that insulin inhibits nuclear PP-2A activity, and that the carboxy-terminal domain of the insulin receptor is important for this effect.
| Reference Key |
draznin1995endocrinologyinsulin
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| Authors | J E Reusch,P Hsieh,P Bhuripanyo,K Carel,J W Leitner,J M Olefsky,B Draznin;J E Reusch;P Hsieh;P Bhuripanyo;K Carel;J W Leitner;J M Olefsky;B Draznin; |
| Journal | endocrinology |
| Year | 1995 |
| DOI |
10.1210/endo.136.6.7750468
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| URL | |
| Keywords |
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