Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis
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Andrew R. Kusmierczyk
Abstract
The 26S proteasome is the key eukaryotic protease responsible for the degradation of intracellular proteins. Protein degradation by the 26S proteasome plays important roles in numerous cellular processes, including the cell cycle, differentiation, apoptosis, and the removal of damaged or misfolded proteins. How this 2.5-MDa complex, composed of at least 32 different polypeptides, is assembled in the first place is not well understood. However, it has become evident that this complicated task is facilitated by a framework of protein factors that chaperone the nascent proteasome through its various stages of assembly. We review here the known proteasome-specific assembly factors, most only recently discovered, and describe their potential roles in proteasome assembly, with an emphasis on the many remaining unanswered questions about this intricate process of assisted self-assembly.
©2008 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Review
- Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis
- Protein Structure and Function
- The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme
- Fluoride complexes of oncogenic Ras mutants to study the Ras-RasGAP interaction
- Docking of tryptophan analogs to trytophanyl-tRNA synthetase: implications for non-canonical amino acid incorporations
- Molecular mechanisms of aromatase inhibition by new A, D-ring modified steroids
- A common binding motif for various bacteria of the bacteria-binding peptide SRCRP2 of DMBT1/gp-340/salivary agglutinin
- Putative identification of an amphipathic α-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation
- Proteolysis
- Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis
- Cleaved SLPI, a novel biomarker of chymase activity
- Expression of tissue and plasma kallikreins and kinin B1 and B2 receptors in lung cancer
- Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis
- Novel Techniques
- Fast in vitro translation system immobilized on a surface via specific biotinylation of the ribosome
Articles in the same Issue
- Review
- Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis
- Protein Structure and Function
- The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme
- Fluoride complexes of oncogenic Ras mutants to study the Ras-RasGAP interaction
- Docking of tryptophan analogs to trytophanyl-tRNA synthetase: implications for non-canonical amino acid incorporations
- Molecular mechanisms of aromatase inhibition by new A, D-ring modified steroids
- A common binding motif for various bacteria of the bacteria-binding peptide SRCRP2 of DMBT1/gp-340/salivary agglutinin
- Putative identification of an amphipathic α-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation
- Proteolysis
- Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis
- Cleaved SLPI, a novel biomarker of chymase activity
- Expression of tissue and plasma kallikreins and kinin B1 and B2 receptors in lung cancer
- Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis
- Novel Techniques
- Fast in vitro translation system immobilized on a surface via specific biotinylation of the ribosome
