4.7 Review

Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles

Journal

BIOMOLECULES
Volume 12, Issue 6, Pages -

Publisher

MDPI
DOI: 10.3390/biom12060764

Keywords

allostery; proteasome; assembly; AAA+ ATPase; proteolysis; ubiquitin; hybrid

Funding

  1. NIH [NCI 1U54CA243126, R35GM140847]

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Allostery-regulation at distant sites is a crucial concept in biology, and the proteasome provides multiple examples of this regulation. It can span a long distance, influencing the interactions and assembly of proteasome modules, and explain how diverse populations of proteasome assemblies are built and maintained in cells.
Allostery-regulation at distant sites is a key concept in biology. The proteasome exhibits multiple forms of allosteric regulation. This regulatory communication can span a distance exceeding 100 angstrom ngstroms and can modulate interactions between the two major proteasome modules: its core particle and regulatory complexes. Allostery can further influence the assembly of the core particle with regulatory particles. In this focused review, known and postulated interactions between these proteasome modules are described. Allostery may explain how cells build and maintain diverse populations of proteasome assemblies and can provide opportunities for therapeutic interventions.

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