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ProteomicsOpen-Gate Mutants of the Mammalian Proteasome Show Enhanced Ubiquitin-Conjugate Degradation
When in the closed form, the axial substrate translocation channel of the proteasome core particle (CP) is topologically blocked by the convergent N-termini of subunits. To probe the role of channel gating in mammalian proteasomes, we have deleted the N-terminal tail of 3. The resulting 3N proteaso...
ORGANISM(S): Homo sapiens (Human) 
2016-03-01 | PXD003577 | Pride
Proteasome Proteomics Gate Tau Oxidative stress Aggregation 
UnknownMechanism of proteasome gate modulation by assembly chaperones Pba1 and Pba2.
Not available
S-EPMC9065996 | biostudies-literature
UnknownOpen-gate mutants of the mammalian proteasome show enhanced ubiquitin-conjugate degradation.
Not available
S-EPMC4786872 | biostudies-literature
UnknownUbiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening.
Not available
S-EPMC2796264 | biostudies-literature
UnknownBlm10 binds to pre-activated proteasome core particles with open gate conformation.
Not available
S-EPMC2603454 | biostudies-literature
UnknownStructure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening.
Not available
S-EPMC2859072 | biostudies-literature
UnknownMechanism of gate opening in the 20S proteasome by the proteasomal ATPases.
Not available
S-EPMC4141531 | biostudies-literature
UnknownProteasome substrate capture and gate opening by the accessory factor PafE from Mycobacterium tuberculosis.
Not available
S-EPMC5880150 | biostudies-literature
ProteomicsStructures of the 26S proteasome in complex with the Hsp70 cochaperone Bag1 reveal a novel mechanism for direct transfer of substrates to the catalytic chamber
Coupling of the degradation and chaperone systems, particularly under cellular stress, is essential for eliminating unfolded proteins. The co-chaperone Bag1 links the Hsp70 chaperone to the 26S proteasome, recruiting Hsp70-bound unfolded proteins for proteasomal degradation. Here, we present cryo-EM...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2025-12-23 | PXD069071 | Pride
Chaperones Degradation Hsp70 Bag1 Proteasome 
UnknownCryo-EM structures of the human PA200 and PA200-20S complex reveal regulation of proteasome gate opening and two PA200 apertures.
Not available
S-EPMC7077846 | biostudies-literature
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