Regulation of EGF receptor dynamics by protein tyrosine phosphatases
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Summary
A new compartmentalized mechanistic model of EGFR phosphorylation dynamics is developed and used to interpret quantitative biochemical measurements to show that EGFR is dephosphorylated at the plasma membrane and in the cell interior with a time scale that is small compared to the time scales for EGFR internalization, which provides new quantitative understanding of how EGFR participates in a number of simultaneous processes that compete for EG FR Cterminal phosphotyrosines.
- Type
- article
- Published
- 2013-01-01
- Cited by
- 0
- References
- 214
- Access
- Open access
- OpenAlex
- https://openalex.org/W1565342892
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:83276166
Keywords
Dephosphorylation, Internalization, Phosphorylation, Epidermal growth factor receptor, Cell biology
References
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- Binding, internalization, and intracellular processing of protein ligands. Derivation of rate constants by computer modeling.
- pH in the endosome. Measurements during pinocytosis and receptor-mediated endocytosis.
- Isolation and characterization of two growth factor-stimulated protein kinases that phosphorylate the epidermal growth factor receptor at threonine 669.
- Differential activities of protein tyrosine phosphatases in intact cells.
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