The mechanism of membrane-associated steps in tail-anchored protein insertion
about
Deubiquitinases sharpen substrate discrimination during membrane protein degradation from the EREndoplasmic reticulum targeting and insertion of tail-anchored membrane proteins by the GET pathwaySubcellular Partitioning of Protein Tyrosine Phosphatase 1B to the Endoplasmic Reticulum and Mitochondria Depends Sensitively on the Composition of Its Tail AnchorStructure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteinsTail-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 Get4Structure of the Sgt2 dimerization domain complexed with the Get5 UBL domain involved in the targeting of tail-anchored membrane proteins to the endoplasmic reticulumStructural and functional characterization of ybr137wp implicates its involvement in the targeting of tail-anchored proteins to membranes.The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteinsThe protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions.In search of tail-anchored protein machinery in plants: reevaluating the role of arsenite transporters.Msp1/ATAD1 maintains mitochondrial function by facilitating the degradation of mislocalized tail-anchored proteinsMPIase is a glycolipozyme essential for membrane protein integration.Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathwayThe protein translocation systems in plants - composition and variability on the example of Solanum lycopersicumThe 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.Interaction surface and topology of Get3-Get4-Get5 protein complex, involved in targeting tail-anchored proteins to endoplasmic reticulum.Epstein-Barr viral BNLF2a protein hijacks the tail-anchored protein insertion machinery to block antigen processing by the transport complex TAP.Trafficking of protein into the recently established photosynthetic organelles of Paulinella chromatophora.Nucleotide-dependent mechanism of Get3 as elucidated from free energy calculations.The complex process of GETting tail-anchored membrane proteins to the ER.A YidC-like Protein in the Archaeal Plasma Membrane.TRC40 can deliver short secretory proteins to the Sec61 translocon.Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein Targeting.Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domainsGet3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked.Precise timing of ATPase activation drives targeting of tail-anchored proteins.Mutation of wrb, a Component of the Guided Entry of Tail-Anchored Protein Pathway, Disrupts Photoreceptor Synapse Structure and Function.Tail-anchored membrane protein insertion into the endoplasmic reticulum.Loss of GET pathway orthologs in Arabidopsis thaliana causes root hair growth defects and affects SNARE abundance.A portrait of the GET pathway as a surprisingly complicated young man.BAG6/BAT3: emerging roles in quality control for nascent polypeptides.Direct targeting of proteins from the cytosol to organelles: the ER versus endosymbiotic organelles.Bag6/Bat3/Scythe: a novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation.All roads lead to Rome (but some may be harder to travel): SRP-independent translocation into the endoplasmic reticulum.BAG-6, a jack of all trades in health and disease.Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins.The emerging role of calcium-modulating cyclophilin ligand in posttranslational insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
P2860
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P2860
The mechanism of membrane-associated steps in tail-anchored protein insertion
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The mechanism of membrane-associated steps in tail-anchored protein insertion
@ast
The mechanism of membrane-associated steps in tail-anchored protein insertion
@en
The mechanism of membrane-associated steps in tail-anchored protein insertion
@nl
type
label
The mechanism of membrane-associated steps in tail-anchored protein insertion
@ast
The mechanism of membrane-associated steps in tail-anchored protein insertion
@en
The mechanism of membrane-associated steps in tail-anchored protein insertion
@nl
prefLabel
The mechanism of membrane-associated steps in tail-anchored protein insertion
@ast
The mechanism of membrane-associated steps in tail-anchored protein insertion
@en
The mechanism of membrane-associated steps in tail-anchored protein insertion
@nl
P2093
P2860
P3181
P356
P1433
P1476
The mechanism of membrane-associated steps in tail-anchored protein insertion
@en
P2093
Agnieszka Mateja
Malaiyalam Mariappan
Malgorzata Dobosz
Robert J Keenan
P2860
P2888
P3181
P356
10.1038/NATURE10362
P407
P577
2011-08-24T00:00:00Z
P6179
1018331154