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• W1570363559 startingPage "3881" @default.
• W1570363559 abstract "The hepatocyte growth factor-regulated tyrosine kinase substrate Hrs is an early endosomal protein that is thought to play a regulatory role in the trafficking of growth factor/receptor complexes through early endosomes. Stimulation of cells with epidermal growth factor (EGF) rapidly leads to phosphorylation of Hrs, raising the question whether the receptor tyrosine kinase phosphorylates Hrs directly. Here, we present evidence that a downstream kinase, rather than the active receptor kinase is responsible. We show that the nonreceptor tyrosine kinase Src is able to phosphorylate Hrs in vitro and in vivo, but that Hrs is nevertheless phosphorylated in Src-, Yes- and Fyn-negative cells. Moreover, we show that only 10-20% of Hrs is phosphorylated following EGF stimulation, and that phosphorylation occurs at multiple tyrosines located in different parts of Hrs. These results suggest that Hrs is a substrate for several kinases downstream of the EGF receptor." @default.
• W1570363559 created "2016-06-24" @default.
• W1570363559 creator A5012473938 @default.
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• W1570363559 creator A5049969358 @default.
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• W1570363559 date "2002-07-31" @default.
• W1570363559 modified "2023-10-18" @default.
• W1570363559 title "Phosphorylation of Hrs downstream of the epidermal growth factor receptor" @default.
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• W1570363559 doi "https://doi.org/10.1046/j.1432-1033.2002.03046.x" @default.
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