Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.
about
Mammalian Sec61 is associated with Sec62 and Sec63Profile of Tom A. Rapoport.Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function predictionMultiple interactions of components mediating preprotein translocation across the inner mitochondrial membraneStructure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localizationAnalysis of mRNA with microsomal fractionation using a SAGE-based DNA microarray system facilitates identification of the genes encoding secretory proteinsAn intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradationThe similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevanceThe Aspergillus nidulans peripheral ER: disorganization by ER stress and persistence during mitosisThe protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membraneX-ray structure of a protein-conducting channelThe mechanism of membrane-associated steps in tail-anchored protein insertionA role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum.Two yeast La motif-containing proteins are RNA-binding proteins that associate with polyribosomes.Structural studies and the assembly of the heptameric post-translational translocon complexThe yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity.Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation.Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiaeSec61p is part of the endoplasmic reticulum-associated degradation machinerySec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.The protein translocation channel binds proteasomes to the endoplasmic reticulum membraneSubunits of the translocon interact with components of the oligosaccharyl transferase complex.A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursorsFunctional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex beta-subunit.Use1p is a yeast SNARE protein required for retrograde traffic to the ER.An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.The homologue of mammalian SPC12 is important for efficient signal peptidase activity in Saccharomyces cerevisiae.The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocationDisruption of YHC8, a member of the TSR1 gene family, reveals its direct involvement in yeast protein translocation.The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degronRer1p as common machinery for the endoplasmic reticulum localization of membrane proteins.Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein importBiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo.A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiaeDifferential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae.Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy.Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum.
P2860
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P248
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P2860
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.
description
1995 nî lūn-bûn
@nan
1995 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@ast
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@en
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@nl
type
label
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@ast
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@en
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@nl
prefLabel
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@ast
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@en
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@nl
P2093
P1433
P1476
Posttranslational protein tran ...... lex of Sec proteins and Kar2p.
@en
P2093
P304
P356
10.1016/0092-8674(95)90077-2
P407
P50
P577
1995-05-19T00:00:00Z