Hsp70–Hsp110 chaperones deliver ubiquitin-dependent and -independent substrates to the 26S proteasome for proteolysis in yeast

Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70

(2018) Naveen K. C. Gowda et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70

(2018) Naveen K. C. Gowda et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae

(2017) Jayasankar Mohanakrishnan Kaimal et al.   MOLECULAR AND CELLULAR BIOLOGY

Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone Sse1 is not obligate for its biological activities

(2017) Veronica M. Garcia et al.   MOLECULAR BIOLOGY OF THE CELL

The requirements of yeast Hsp70 of SSA family for the ubiquitin-dependent degradation of short-lived and abnormal proteins

(2016) Do Hee Lee et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

The recognition of ubiquitinated proteins by the proteasome

(2016) Guinevere L. Grice et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Ubiquitin‐like domains can target to the proteasome but proteolysis requires a disordered region

(2016) Houqing Yu et al.   EMBO JOURNAL

The Proteasome Subunit Rpn8 Interacts with the Small Nucleolar RNA Protein (snoRNP) Assembly Protein Pih1 and Mediates Its Ubiquitin-independent Degradation inSaccharomyces cerevisiae

(2016) Alexandr Paci et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Conserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome

(2016) Houqing Yu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast

(2016) Naveen Kumar Chandappa Gowda et al.   MOLECULAR BIOLOGY OF THE CELL

Luciferase NanoLuc as a reporter for gene expression and protein levels inSaccharomyces cerevisiae

(2016) Anna E. Masser et al.   YEAST

Ubiquitylation Directly Induces Fold Destabilization of Proteins

(2016) Daichi Morimoto et al.   Scientific Reports

Sequence composition of disordered regions fine-tunes protein half-life

(2015) Susan Fishbain et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates

(2015) Daichi Morimoto et al.   Nature Communications

Sequence composition of disordered regions fine-tunes protein half-life

(2015) Susan Fishbain et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Hierarchical Functional Specificity of Cytosolic Heat Shock Protein 70 (Hsp70) Nucleotide Exchange Factors in Yeast

(2014) Jennifer L. Abrams et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress

(2014) Nancy N. Fang et al.   NATURE CELL BIOLOGY

Ubiquitin-independent proteasomal degradation

(2013) Jenny Erales et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

The Cotranslational Function of Ribosome-Associated Hsp70 in Eukaryotic Protein Homeostasis

(2013) Felix Willmund et al.   CELL

Hsp70 Targets a Cytoplasmic Quality Control Substrate to the San1p Ubiquitin Ligase

(2013) Christopher J. Guerriero et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

System-wide Analysis Reveals Intrinsically Disordered Proteins Are Prone to Ubiquitylation after Misfolding Stress

(2013) Alex H. M. Ng et al.   MOLECULAR & CELLULAR PROTEOMICS

Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting

(2013) Ayala Shiber et al.   MOLECULAR BIOLOGY OF THE CELL

Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

(2013) Stéphanie Escusa-Toret et al.   NATURE CELL BIOLOGY

Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins

(2013) N. K. C. Gowda et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

A Network of Ubiquitin Ligases Is Important for the Dynamics of Misfolded Protein Aggregates in Yeast

(2012) Maria A. Theodoraki et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Structure of Minimal Tetratricopeptide Repeat Domain Protein Tah1 Reveals Mechanism of Its Interaction with Pih1 and Hsp90

(2011) Beatriz Jiménez et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The N-Terminal Unstructured Domain of Yeast ODC Functions as a Transplantable and Replaceable Ubiquitin-Independent Degron

(2011) Daniela Gödderz et al.   JOURNAL OF MOLECULAR BIOLOGY

Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins

(2011) Nancy N. Fang et al.   NATURE CELL BIOLOGY

A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes

(2010) Ansgar Koplin et al.   JOURNAL OF CELL BIOLOGY

The Prodomain of Ssy5 Protease Controls Receptor-Activated Proteolysis of Transcription Factor Stp1

(2010) T. Pfirrmann et al.   MOLECULAR AND CELLULAR BIOLOGY

Hsp110 Chaperones Control Client Fate Determination in the Hsp70–Hsp90 Chaperone System

(2010) Atin K. Mandal et al.   MOLECULAR BIOLOGY OF THE CELL

Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding

(2010) T. Hagai et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation

(2009) Vivian Su et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1

(2009) J. W. Heck et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding

(2008) Sigrun Polier et al.   CELL

Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1

(2008) Frederik Eisele et al.   FEBS LETTERS

Hsp110 Is a Nucleotide-activated Exchange Factor for Hsp70

(2008) Claes Andréasson et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Proteasome subunit Rpn13 is a novel ubiquitin receptor

(2008) Koraljka Husnjak et al.   NATURE

Misfolded proteins partition between two distinct quality control compartments

(2008) Daniel Kaganovich et al.   NATURE

Hsp110 Chaperones Regulate Prion Formation and Propagation in S. cerevisiae by Two Discrete Activities

(2008) Heather Sadlish et al.   PLoS One

Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity

(2008) C. Andreasson et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA