In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
about
A heritable switch in carbon source utilization driven by an unusual yeast prionMolecular chaperones: guardians of the proteome in normal and disease statesDisaggregases, molecular chaperones that resolubilize protein aggregatesModulation and elimination of yeast prions by protein chaperones and co-chaperonesThe [RNQ+] prion: a model of both functional and pathological amyloidStructural basis for intersubunit signaling in a protein disaggregating machineMolecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Yeast prions are useful for studying protein chaperones and protein quality controlCooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationThe biological functions of Naa10 - From amino-terminal acetylation to human diseaseGPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells.Laser-induced propagation and destruction of amyloid beta fibrils.Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress.The Hsp104 N-terminal domain enables disaggregase plasticity and potentiationThe Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.Modeling Huntington disease in yeast: perspectives and future directions.Influence of prion variant and yeast strain variation on prion-molecular chaperone requirementsSubstrate Discrimination by ClpB and Hsp104.Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs.Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seedsOverexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network of Arabidopsis thaliana[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation.Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variantsThe mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free systemPrion propagation can occur in a prokaryote and requires the ClpB chaperone.The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner.Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation.Defining the limits: Protein aggregation and toxicity in vivoThe Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availabilitySpatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation.Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.Destabilization and recovery of a yeast prion after mild heat shock.
P2860
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P2860
In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
description
2008 nî lūn-bûn
@nan
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
In vivo monitoring of the prio ...... elivering substrates to Hsp104
@ast
In vivo monitoring of the prio ...... elivering substrates to Hsp104
@en
type
label
In vivo monitoring of the prio ...... elivering substrates to Hsp104
@ast
In vivo monitoring of the prio ...... elivering substrates to Hsp104
@en
prefLabel
In vivo monitoring of the prio ...... elivering substrates to Hsp104
@ast
In vivo monitoring of the prio ...... elivering substrates to Hsp104
@en
P2860
P1433
P1476
In vivo monitoring of the prio ...... elivering substrates to Hsp104
@en
P2093
Katherine J Verges
Kimberly A Tipton
P2860
P304
P356
10.1016/J.MOLCEL.2008.11.003
P577
2008-11-01T00:00:00Z