Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.
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A ribosome-associating factor chaperones tail-anchored membrane proteinsPromotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated proteinModel for eukaryotic tail-anchored protein binding based on the structure of Get3Structural insights into tail-anchored protein binding and membrane insertion by Get3The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesisStructural characterization of the Get4/Get5 complex and its interaction with Get3A Conserved Archaeal Pathway for Tail-Anchored Membrane Protein InsertionStructural Basis for Tail-Anchored Membrane Protein Biogenesis by the Get3-Receptor ComplexThe mechanism of membrane-associated steps in tail-anchored protein insertionTail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologueCrystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4Structural and functional characterization of ybr137wp implicates its involvement in the targeting of tail-anchored proteins to membranes.A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum.The GET complex mediates insertion of tail-anchored proteins into the ER membrane.Comprehensive characterization of genes required for protein folding in the endoplasmic reticulumErgosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes.The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions.SGTA antagonizes BAG6-mediated protein triageThe SND proteins constitute an alternative targeting route to the endoplasmic reticulum.Helix insertion into bilayers and the evolution of membrane proteins.Bacterial transmembrane proteins that lack N-terminal signal sequences.The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum.Metabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion proteinMembrane protein insertion at the endoplasmic reticulum.The association of BAG6 with SGTA and tail-anchored proteinsWRB and CAML are necessary and sufficient to mediate tail-anchored protein targeting to the ER membrane.The Get1/2 transmembrane complex is an endoplasmic-reticulum membrane protein insertase.Epstein-Barr viral BNLF2a protein hijacks the tail-anchored protein insertion machinery to block antigen processing by the transport complex TAP.Nucleotide-dependent mechanism of Get3 as elucidated from free energy calculations.TRC40 can deliver short secretory proteins to the Sec61 translocon.Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targetingGet3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked.Peroxin-dependent targeting of a lipid-droplet-destined membrane protein to ER subdomainsTail-anchored membrane protein insertion into the endoplasmic reticulum.Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane.Protein disulfide isomerase-2 of Arabidopsis mediates protein folding and localizes to both the secretory pathway and nucleus, where it interacts with maternal effect embryo arrest factor.Biogenesis of tail-anchored proteins: the beginning for the end?Physiological and environmental control of yeast prions.A portrait of the GET pathway as a surprisingly complicated young man.Secretory protein biogenesis and traffic in the early secretory pathway
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P2860
Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 13 May 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.
@en
Distinct targeting pathways for the membrane insertion of tail-anchored
@nl
type
label
Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.
@en
Distinct targeting pathways for the membrane insertion of tail-anchored
@nl
prefLabel
Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.
@en
Distinct targeting pathways for the membrane insertion of tail-anchored
@nl
P2093
P2860
P356
P1476
Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.
@en
P2093
Bernhard Dobberstein
Milan Spasic
Vincenzo Favaloro
P2860
P304
P356
10.1242/JCS.020321
P407
P577
2008-05-13T00:00:00Z