Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation

Mol Cell. 2006 May 5;22(3):317-27. doi: 10.1016/j.molcel.2006.04.007.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Cycle / physiology
  • Cells, Cultured
  • Cysteine Endopeptidases / metabolism*
  • Gene Expression Regulation
  • Humans
  • K562 Cells
  • Mice
  • Models, Biological
  • Oxidative Stress
  • Phosphorylation
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Binding
  • Protein Processing, Post-Translational*
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins c-abl / metabolism*
  • Radiation, Ionizing

Substances

  • ARG tyrosine kinase
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins c-abl
  • Cysteine Endopeptidases
  • PSMA7 protein, human
  • Proteasome Endopeptidase Complex