The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.
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Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 functionInteraction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasomeCross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysisRad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chainsInvolvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalphaThe UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiaeUbiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasomeDevelopmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomesUbiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradationUse of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysisThe life cycle of the 26S proteasome: from birth, through regulation and function, and onto its deathThe recognition of ubiquitinated proteins by the proteasomeMitochondrial and Ubiquitin Proteasome System Dysfunction in Ageing and Disease: Two Sides of the Same Coin?Graded Proteasome Dysfunction in Caenorhabditis elegans Activates an Adaptive Response Involving the Conserved SKN-1 and ELT-2 Transcription Factors and the Autophagy-Lysosome PathwayDeubiquitylation machinery is required for embryonic polarity in Caenorhabditis elegansStructure and ubiquitin binding of the ubiquitin-interacting motifBinding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5aStructure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23BStructure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12Molecular architecture and assembly of the eukaryotic proteasomeProteasome subunit Rpn1 binds ubiquitin-like protein domains.A genetic screen for Saccharomyces cerevisiae mutants affecting proteasome function, using a ubiquitin-independent substrate.Rpn9 is required for efficient assembly of the yeast 26S proteasomeSts1 plays a key role in targeting proteasomes to the nucleus.Functional analysis of Rpn6p, a lid component of the 26 S proteasome, using temperature-sensitive rpn6 mutants of the yeast Saccharomyces cerevisiae.Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomesSubunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome.Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway.Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome.An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network.Rpn7 Is required for the structural integrity of the 26 S proteasome of Saccharomyces cerevisiae.Functional characterization of rpn3 uncovers a distinct 19S proteasomal subunit requirement for ubiquitin-dependent proteolysis of cell cycle regulatory proteins in budding yeast.Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasomeA genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradationPhysical association of ubiquitin ligases and the 26S proteasome.
P2860
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P2860
The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@ast
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@en
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@nl
type
label
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@ast
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@en
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@nl
altLabel
The multiubiquitin-chain-bindi ...... cific role in protein turnover
@en
prefLabel
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@ast
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@en
The multiubiquitin-chain-bindi ...... ific role in protein turnover.
@nl
P2093
P2860
P3181
P356
P1476
The multiubiquitin-chain-bindi ...... cific role in protein turnover
@en
P2093
R D Vierstra
S van Nocker
P2860
P304
P3181
P356
10.1128/MCB.16.11.6020
P407
P577
1996-11-01T00:00:00Z