Tyrosine phosphorylation of NEDD4 activates its ubiquitin ligase activity

• DOI: 10.1126/scisignal.2005290
• Publication Date: 2014-10-07T22:28:24Z
• Authors: Avinash Persaud; Philipp Alberts; Sara Mari; Jiefei Tong; Ryan Murchie; Elena Maspero; Frozan Safi; Michael F. Moran; Simona Polo; Daniela Rotin
• Keywords: Models, Molecular; 0301 basic medicine; DNA, Complementary; Endosomal Sorting Complexes Required for Transport; Epidermal Growth Factor; Nedd4 Ubiquitin Protein Ligases; Ubiquitin-Protein Ligases; Enzyme-Linked Immunosorbent Assay; Receptor Cross-Talk; Real-Time Polymerase Chain Reaction; Endocytosis; 03 medical and health sciences; Tandem Mass Spectrometry; Gene Knockdown Techniques; Proteolysis; growth-factor receptor; SRC-family kinases; C2 domain; binding-site; EGF receptor; complex; endocytosis; monoubiquitination; electrostatics; localization; Mutagenesis, Site-Directed; Humans; Immunoprecipitation; Tyrosine; Receptor, Fibroblast Growth Factor, Type 1; Phosphorylation; HeLa Cells

The receptor tyrosine kinases FGFR1 and EGFR promote phosphorylation of the ubiquitin ligase NEDD4, leading to activation of its catalytic activity.