IndraLab

Statements

Ubiquitin binds PSMD14. 7 / 7
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sparser
"Notably, states E A1 and E A2 show ubiquitin densities near RPN10 and RPN11 and no substrate density inside the AAA ring, whereas state E B shows density features of both RPN11-bound ubiquitin and AAA-bound substrate with a visible isopeptide bond between the ubiquitin and substrate."
32325699
sparser
"In contrast, state E C1 shows densities of both RPN11-bound ubiquitin and AAA-bound substrate, with the isopeptide bond being completely absent in density, unambiguously verifying that this state is chemically post-deubiquitylation following state E B . Interestingly, state E C2 shows virtually identical ATPase conformation but lacks the RPN11-bound ubiquitin and the nucleotide density in RPT1, thus verifying that it represents the state immediately after state E C1 ."
32325699
sparser
"In contrast to the RPN11-bound ubiquitin in statesand, no ubiquitin was observed on RPN11 in any state in which USP14 is engaged with ubiquitin (Fig. xref , Extended Data Figs. xref a, xref ), suggesting that activated USP14 and RPN11 do not bind ubiquitin simultaneously."
35477760
sparser
"In support of this model, all S D -like and E D -like states of the USP14-bound proteasome showed no ubiquitin binding to RPN11."
35477760
sparser
"Notably, this RPN11-bound ubiquitin in E A2.1 clearly shows higher resolution features consistent with 3.8 Å, with sufficiently separated β-strands ( xref D)."
36012133
sparser
"This is in contrast to RPN11 in all the USP14-free E D -like states xref , which exhibit no RPN11-bound ubiquitin, implying rapid release of cleaved ubiquitin."
35477760
sparser
"Around the scissile isopeptide bond between the RPN11-bound ubiquitin and the substrate lysine, a ternary interface is formed between RPN11, RPN8 and the N-loop of RPT5 which emanates from the top of its OB domain to efficiently carry out the deubiquitylation step ( xref b) [ xref ]."
32325699