Regulatory subunit interactions of the 26S proteasome, a complex problem.
The 26S proteasome is the major non-lysosomal protease in eukaryotic cells. This multimeric enzyme is the integral component of the ubiquitin-mediated substrate degradation pathway. It consists of two subcomplexes, the 20S proteasome, which forms the proteolytic core, and the 19S regulator (or PA700), which confers ATP dependency and ubiquitinated substrate specificity on the enzyme. Recent biochemical and genetic studies have revealed many of the interactions between the 17 regulatory subunits, yielding an approximation of the 19S complex topology. Inspection of interactions of regulatory subunits with non-subunit proteins reveals patterns that suggest these interactions play a role in 26S proteasome regulation and localization.
Ferrell
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Dept of Biochemistry, University of Utah, 50 N. Medical Drive, Salt Lake City, UT 84132, USA.
Wilkinson
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Dubiel
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Gordon
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D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D006801:Humans; D010447:Peptide Hydrolases / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D011506:Proteins / Q000378:metabolism; D016601:RNA-Binding Proteins; D013045:Species Specificity
D002352:Carrier Proteins; C085834:PA700 proteasome activator; C498506:PSMD4 protein, human; D011506:Proteins; D016601:RNA-Binding Proteins; D010447:Peptide Hydrolases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease; D000251:Adenosine Triphosphatases