Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation.
Proteasome-mediated proteolysis is a primary protein degradation pathway in cells. The present study demonstrates that c-Abl and Arg (abl-related gene) tyrosine kinases associate with and phosphorylate the proteasome PSMA7 (alpha4) subunit at Tyr-153. Consequently, proteasome-dependent proteolysis is compromised. Notably, cells expressing a phosphorylation mutant of PSMA7(Y153F) display impaired G1/S transition ... and S/G2 progression, highlighting the biological significance of tyrosine phosphorylation of a proteasome subunit as an important cellular regulatory control.
Mesh Terms:
Animals, Cell Cycle, Cells, Cultured, Cysteine Endopeptidases, Gene Expression Regulation, Humans, K562 Cells, Mice, Models, Biological, Oxidative Stress, Phosphorylation, Proteasome Endopeptidase Complex, Protein Binding, Protein Processing, Post-Translational, Protein-Tyrosine Kinases, Proto-Oncogene Proteins c-abl, Radiation, Ionizing
Animals, Cell Cycle, Cells, Cultured, Cysteine Endopeptidases, Gene Expression Regulation, Humans, K562 Cells, Mice, Models, Biological, Oxidative Stress, Phosphorylation, Proteasome Endopeptidase Complex, Protein Binding, Protein Processing, Post-Translational, Protein-Tyrosine Kinases, Proto-Oncogene Proteins c-abl, Radiation, Ionizing
Mol. Cell
Date: May. 05, 2006
PubMed ID: 16678104
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