Proteostasis impairment in protein-misfolding and-aggregation diseases
Cells possess an extensive network of components to safeguard proteome integrity and
maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines …
maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines …
[HTML][HTML] Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system
I Amm, T Sommer, DH Wolf - … et Biophysica Acta (BBA)-Molecular Cell …, 2014 - Elsevier
Mistakes are part of our world and constantly occurring. Due to transcriptional and
translational failures, genomic mutations or diverse stress conditions like oxidation or heat …
translational failures, genomic mutations or diverse stress conditions like oxidation or heat …
Mechanisms and functions of spatial protein quality control
A healthy proteome is essential for cell survival. Protein misfolding is linked to a rapidly
expanding list of human diseases, ranging from neurodegenerative diseases to aging and …
expanding list of human diseases, ranging from neurodegenerative diseases to aging and …
PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone
Dysfunction of protein quality control contributes to the cellular pathology of polyglutamine
(polyQ) expansion diseases and other neurodegenerative disorders associated with …
(polyQ) expansion diseases and other neurodegenerative disorders associated with …
Distinct proteostasis circuits cooperate in nuclear and cytoplasmic protein quality control
Protein misfolding is linked to a wide array of human disorders, including Alzheimer's
disease, Parkinson's disease and type II diabetes,. Protective cellular protein quality control …
disease, Parkinson's disease and type II diabetes,. Protective cellular protein quality control …
Failure of RQC machinery causes protein aggregation and proteotoxic stress
Translation of messenger RNAs lacking a stop codon results in the addition of a carboxy-
terminal poly-lysine tract to the nascent polypeptide, causing ribosome stalling. Non-stop …
terminal poly-lysine tract to the nascent polypeptide, causing ribosome stalling. Non-stop …
Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope
AB Mehrtash, M Hochstrasser - Seminars in cell & developmental biology, 2019 - Elsevier
Numerous nascent proteins undergo folding and maturation within the luminal and
membrane compartments of the endoplasmic reticulum (ER). Despite the presence of …
membrane compartments of the endoplasmic reticulum (ER). Despite the presence of …
Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress
NN Fang, GT Chan, M Zhu, SA Comyn, A Persaud… - Nature cell …, 2014 - nature.com
The heat-shock response is a complex cellular program that induces major changes in
protein translation, folding and degradation to alleviate toxicity caused by protein misfolding …
protein translation, folding and degradation to alleviate toxicity caused by protein misfolding …
Proteotoxicity from aberrant ribosome biogenesis compromises cell fitness
To achieve maximal growth, cells must manage a massive economy of ribosomal proteins (r-
proteins) and RNAs (rRNAs) to produce thousands of ribosomes every minute. Although …
proteins) and RNAs (rRNAs) to produce thousands of ribosomes every minute. Although …
Chaperoning proteins for destruction: diverse roles of Hsp70 chaperones and their co-chaperones in targeting misfolded proteins to the proteasome
Molecular chaperones were originally discovered as heat shock-induced proteins that
facilitate proper folding of proteins with non-native conformations. While the function of …
facilitate proper folding of proteins with non-native conformations. While the function of …