Bat3 promotes the membrane integration of tail-anchored proteins.
about
A ribosome-associating factor chaperones tail-anchored membrane proteinsCytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradationSGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradationStructural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein AlphaModification by ubiquitin-like proteins: significance in apoptosis and autophagy pathwaysA Conserved Archaeal Pathway for Tail-Anchored Membrane Protein InsertionThe mechanism of membrane-associated steps in tail-anchored protein insertionStructures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic InterfaceGet5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 ComplexInteractome profile of the host cellular proteins and the nonstructural protein 2 of porcine reproductive and respiratory syndrome virusSolution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4ASGTA antagonizes BAG6-mediated protein triageA soluble fragment of the tumor antigen BCL2-associated athanogene 6 (BAG-6) is essential and sufficient for inhibition of NKp30 receptor-dependent cytotoxicity of natural killer cellsEnzymatic blockade of the ubiquitin-proteasome pathwayBAT3 guides misfolded glycoproteins out of the endoplasmic reticulum.Membrane protein insertion at the endoplasmic reticulum.A novel BAT3 sequence generated by alternative RNA splicing of exon 11B displays cell type-specific expression and impacts on subcellular localization.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.Protein targeting and degradation are coupled for elimination of mislocalized proteins.The complex process of GETting tail-anchored membrane proteins to the ER.Proteasomal degradation of preemptive quality control (pQC) substrates is mediated by an AIRAPL-p97 complex.TRC40 can deliver short secretory proteins to the Sec61 translocon.Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targetingTail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway.Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked.A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradationNuclear BAG6-UBL4A-GET4 complex mediates DNA damage signaling and cell death.Glycoproteins gE and gI are required for efficient KIF1A-dependent anterograde axonal transport of alphaherpesvirus particles in neurons.Tail-anchored membrane protein insertion into the endoplasmic reticulum.Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane.Reorientation of the first signal-anchor sequence during potassium channel biogenesis at the Sec61 complex.Tail-anchored membrane proteins: exploring the complex diversity of tail-anchored-protein targeting in plant cells.A portrait of the GET pathway as a surprisingly complicated young man.BAG6/BAT3: emerging roles in quality control for nascent polypeptides.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.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.
P2860
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P2860
Bat3 promotes the membrane integration of tail-anchored proteins.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Bat3 promotes the membrane integration of tail-anchored proteins.
@en
type
label
Bat3 promotes the membrane integration of tail-anchored proteins.
@en
prefLabel
Bat3 promotes the membrane integration of tail-anchored proteins.
@en
P2860
P50
P356
P1476
Bat3 promotes the membrane integration of tail-anchored proteins.
@en
P2093
Pawel Leznicki
P2860
P304
P356
10.1242/JCS.066738
P407
P577
2010-06-01T00:00:00Z