The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein

Mechanisms for cooperation between the cytosolic Hsp70 system and the ubiquitin proteasome system during protein triage are not clear. Herein, we identify new mechanisms for selection of misfolded cytosolic proteins for degradation via defining functional interactions between specific cytosolic Hsp7...

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Veröffentlicht in:	PloS one 2013-01, Vol.8 (1), p.e52099
Hauptverfasser:	Summers, Daniel W, Wolfe, Katie J, Ren, Hong Yu, Cyr, Douglas M
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Amino Acid Sequence Biology Cooperativity Cycloheximide - pharmacology Cytosol - metabolism Degradation Developmental biology Green Fluorescent Proteins - chemistry Green Fluorescent Proteins - metabolism Heat shock proteins Homeostasis HSP40 Heat-Shock Proteins - metabolism Hsp40 protein HSP70 Heat-Shock Proteins - metabolism Hsp70 protein Intermediates Ligases Medicine Molecular Sequence Data Plasmids Proteasome Endopeptidase Complex - metabolism Proteasomes Protein folding Protein Folding - drug effects Protein Stability Proteins Proteolysis - drug effects Quality control Saccharomyces cerevisiae - drug effects Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Substrate Specificity - drug effects Surface active agents Ubiquitin Ubiquitin - metabolism Ubiquitin-protein ligase Ubiquitin-Protein Ligases - metabolism
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