Ubiquitylation of the amino terminus of Myc by SCFβ-TrCP antagonizes SCFFbw7-mediated turnover
Copyright policy )Ubiquitylation of the amino terminus of Myc by SCFβ-TrCP antagonizes SCFFbw7-mediated turnover
The SCFFbw7 ubiquitin ligase mediates growth-factor-regulated turnover of the Myc oncoprotein. Here we show that SCFβ-TrCP binds to Myc by means of a characteristic phosphodegron and ubiquitylates Myc; this results in enhanced Myc stability. SCFFbw7 and SCFβ-TrCP can exert these differential effects through polyubiquitylation of the amino terminus of Myc. Whereas SCFFbw7 with the Cdc34 ubiquitin-conjugating enzyme specifically requires lysine 48 (K48) of ubiquitin, SCFβ-TrCP uses the UbcH5 ubiquitin-conjugating enzyme to form heterotypic polyubiquitin chains on Myc. Ubiquitylation of Myc by SCFβ-TrCP is required for Myc-dependent acceleration of cell cycle progression after release from an arrest in S phase. Therefore, alternative ubiquitylation events at the N terminus can lead to the ubiquitylation-dependent stabilization of Myc.
- University of Würzburg Germany
G2 Phase, F-Box-WD Repeat-Containing Protein 7, F-Box Proteins, Amino Acid Motifs, Cell Cycle Proteins, Protein Serine-Threonine Kinases, Models, Biological, Anaphase-Promoting Complex-Cyclosome, S Phase, Proto-Oncogene Proteins c-myc, Mice, Proto-Oncogene Proteins, Consensus Sequence, NIH 3T3 Cells, Animals, Humans, Polyubiquitin, Cells, Cultured, HeLa Cells, Protein Binding
G2 Phase, F-Box-WD Repeat-Containing Protein 7, F-Box Proteins, Amino Acid Motifs, Cell Cycle Proteins, Protein Serine-Threonine Kinases, Models, Biological, Anaphase-Promoting Complex-Cyclosome, S Phase, Proto-Oncogene Proteins c-myc, Mice, Proto-Oncogene Proteins, Consensus Sequence, NIH 3T3 Cells, Animals, Humans, Polyubiquitin, Cells, Cultured, HeLa Cells, Protein Binding
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