Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast.
about
Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chainsA complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteinsNMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised.The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulumInvolvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitinationIdentification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradationUbiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradationStructural determinants for the binding of ubiquitin-like domains to the proteasomeStructure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23BStructural Requirements for the Ubiquitin-associated Domain of the mRNA Export Factor Mex67 to Bind Its Specific Targets, the Transcription Elongation THO Complex Component Hpr1 and Nucleoporin FXFG RepeatsRad4-Rad23 interaction with SWI/SNF links ATP-dependent chromatin remodeling with nucleotide excision repair.N-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity.Rad4 regulates protein turnover at a postubiquitylation step.Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domainA genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradationEvidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogasterAn investigation of the activity of recombinant rat skeletal muscle cytosolic sialidaseMan2C1, an alpha-mannosidase, is involved in the trimming of free oligosaccharides in the cytosol.N-linked glycosylation does not impair proteasomal degradation but affects class I major histocompatibility complex presentation.Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation.Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasomeA role for N-glycanase in the cytosolic turnover of glycoproteins.Rad23 promotes the targeting of proteolytic substrates to the proteasome.The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder.Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding moduleFor whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Transcription factor Nrf1 is topologically repartitioned across membranes to enable target gene transactivation through its acidic glucose-responsive domainsThe Png1-Rad23 complex regulates glycoprotein turnover.Versatility of the endoplasmic reticulum protein folding factory.Endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins and mutant P23H rhodopsin in photoreceptor cells.The secretory pathway: exploring yeast diversity.Structural features of free N-glycans occurring in plants and functional features of de-N-glycosylation enzymes, ENGase, and PNGase: the presence of unusual plant complex type N-glycans.Site-specific labeling of cytoplasmic peptide:N-glycanase by N,N'-diacetylchitobiose-related compounds.The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity.Generation and degradation of free asparagine-linked glycans.ERADication of EDEM1 occurs by selective autophagy and requires deglycosylation by cytoplasmic peptide N-glycanase.
P2860
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P2860
Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Rad23 provides a link between ...... the 26 S proteasome in yeast.
@en
type
label
Rad23 provides a link between ...... the 26 S proteasome in yeast.
@en
prefLabel
Rad23 provides a link between ...... the 26 S proteasome in yeast.
@en
P2093
P2860
P356
P1476
Rad23 provides a link between ...... d the 26 S proteasome in yeast
@en
P2093
P2860
P304
21601-21607
P356
10.1074/JBC.M100826200
P407
P577
2001-03-20T00:00:00Z