Structure and function of the 26S proteasome
As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal
proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The …
proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The …
The logic of the 26S proteasome
GA Collins, AL Goldberg - Cell, 2017 - cell.com
The ubiquitin proteasome pathway is responsible for most of the protein degradation in
mammalian cells. Rates of degradation by this pathway have generally been assumed to be …
mammalian cells. Rates of degradation by this pathway have generally been assumed to be …
The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates
Proteins are targeted to the proteasome by the attachment of ubiquitin chains, which are
markedly varied in structure. Three proteasome subunits–Rpn10, Rpn13, and Rpn1–can …
markedly varied in structure. Three proteasome subunits–Rpn10, Rpn13, and Rpn1–can …
Structure, dynamics and function of the 26S proteasome
Y Mao - Macromolecular protein complexes III: structure and …, 2021 - Springer
The 26S proteasome is the most complex ATP-dependent protease machinery, of~ 2.5 MDa
mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated …
mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated …
The 26S proteasome utilizes a kinetic gateway to prioritize substrate degradation
The 26S proteasome is the principal macromolecular machine responsible for protein
degradation in eukaryotes. However, little is known about the detailed kinetics and …
degradation in eukaryotes. However, little is known about the detailed kinetics and …
The ubiquitin–proteasome system in kidney physiology and disease
C Meyer-Schwesinger - Nature Reviews Nephrology, 2019 - nature.com
Intracellular proteins continuously turn over by degradation and synthesis in all organ
tissues. Owing to its irreversible nature, protein degradation is a highly selective process to …
tissues. Owing to its irreversible nature, protein degradation is a highly selective process to …
Recognition of client proteins by the proteasome
H Yu, A Matouschek - Annual review of biophysics, 2017 - annualreviews.org
The ubiquitin proteasome system controls the concentrations of regulatory proteins and
removes damaged and misfolded proteins from cells. Proteins are targeted to the protease …
removes damaged and misfolded proteins from cells. Proteins are targeted to the protease …
The ERAD system is restricted by elevated ceramides
Misfolded proteins in the endoplasmic reticulum (ER) are removed through a process known
as ER-associated degradation (ERAD). ERAD occurs through an integral membrane protein …
as ER-associated degradation (ERAD). ERAD occurs through an integral membrane protein …
Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies
The 26S proteasome is responsible for regulated proteolysis in eukaryotic cells. Its
substrates are diverse in structure, function, sequence length, and amino acid composition …
substrates are diverse in structure, function, sequence length, and amino acid composition …
Mechanisms of substrate recognition by the 26S proteasome
C Davis, BL Spaller, A Matouschek - Current opinion in structural biology, 2021 - Elsevier
Highlights•Many types of ubiquitin modification can target proteins to the proteasome for
degradation.•The ubiquitin receptors of the RP individually and cooperatively function to …
degradation.•The ubiquitin receptors of the RP individually and cooperatively function to …