Plasticity in the structure and assembly of proteasomes

Area of Science:

• Molecular Biology
• Structural Biology
• Cell Biology

Background:

• Proteasomes are essential large multisubunit protease complexes regulating protein degradation for organismal health.
• The canonical 26S proteasome comprises a proteolytic core particle (CP) and a regulatory particle (RP) that unfolds and translocates substrates for degradation.
• Proteasome biogenesis is a complex, orchestrated process involving dedicated assembly chaperones.

Purpose of the Study:

• To review the structure and assembly of canonical and non-canonical proteasomes.
• To highlight recent structural studies clarifying proteasome formation.
• To explore assembly mechanisms and plasticity in proteasome subunit composition and pathways.

Main Methods:

• Literature review of structural and assembly studies.
• Analysis of recent structural data on proteasome biogenesis.
• Exploration of emerging evidence on proteasome assembly pathways.

Main Results:

• Recent structural studies have significantly advanced understanding of proteasome assembly.
• Non-canonical proteasome forms with distinct subunit compositions and alternative regulators exist.
• Assembly mechanisms allow for plasticity in proteasome subunit composition and biogenesis pathways.

Conclusions:

• Proteasome assembly is a highly orchestrated yet adaptable process.
• Understanding proteasome biogenesis is crucial for comprehending cellular quality control and organismal health.
• Further research into proteasome assembly plasticity may reveal new therapeutic targets.