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Regulating protein breakdown through proteasome phosphorylation.

Jordan J S VerPlank1, Alfred L Goldberg2

  • 1Harvard Medical School, Boston, MA 02115, U.S.A.

The Biochemical Journal
|September 27, 2017
PubMed
Summary
This summary is machine-generated.

Protein kinase modifications of the 26S proteasome regulate protein degradation. Kinases like PKA and DYRK2 stimulate proteasome activity, while ASK1 inhibits it, offering therapeutic potential for diseases and cancer.

Keywords:
proteasome activationproteasome phosphorylationprotein degradationprotein homeostasisprotein kinaseubiquitin proteasome system

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Medicine

Background:

  • The ubiquitin proteasome system is crucial for protein degradation in mammalian cells.
  • While ubiquitination is a primary regulator, post-translational modifications of the 26S proteasome also impact protein half-lives.
  • Emerging research highlights the role of proteasome subunit phosphorylation in modulating its function.

Purpose of the Study:

  • To review how various kinases alter 26S proteasome function through subunit phosphorylation.
  • To explore the physiological significance of proteasome phosphorylation in cellular processes and disease.
  • To discuss the therapeutic potential of manipulating proteasome phosphorylation for various diseases.

Main Methods:

  • Literature review of studies investigating kinase-mediated proteasome phosphorylation.
  • Analysis of specific kinase examples (PKA, DYRK2, ASK1) and their effects on proteasome activity.
  • Examination of the link between proteasome phosphorylation and cellular signaling pathways.

Main Results:

  • Protein kinase A (PKA) and dual-specificity tyrosine-regulated kinase 2 (DYRK2) stimulate proteasome degradation of proteins, peptides, and ATP.
  • Apoptosis signal-regulating kinase 1 (ASK1) inhibits proteasome function during apoptosis.
  • Proteasome phosphorylation is influenced by hormones, neurotransmitters, cyclic nucleotide levels, calcium influx, and cell cycle phases.
  • Pharmacological activation of PKA/PKG enhances proteasomal degradation of misfolded proteins, showing promise in neurodegenerative and myocardial disease models.
  • Inhibition of DYRK2-mediated phosphorylation slows cell cycle progression and tumor growth.

Conclusions:

  • Proteasome subunit phosphorylation by kinases is a significant regulatory mechanism for protein degradation.
  • This phosphorylation is integrated into key cellular signaling pathways and physiological states.
  • Targeting proteasome phosphorylation offers a promising therapeutic strategy for proteotoxic diseases and cancer, warranting further investigation into specific subunit modifications and their functional consequences.