Corrigendum to “Understanding organellar protein folding capacities and assessing their pharmacological modulation by small molecules” [Eur. J. Cell Biol. 97 (2018) 114–125]

2020 ◽  
Vol 99 (2-3) ◽  
pp. 151074
Author(s):  
Richa Sharma ◽  
Mukund M.D. Pramanik ◽  
Balasubramanian Chandramouli ◽  
Namrata Rastogi ◽  
Niti Kumar
Keyword(s):  
Protein Folding ◽  
Small Molecules ◽  
Pharmacological Modulation ◽  
Cell Biol

Understanding organellar protein folding capacities and assessing their pharmacological modulation by small molecules

2018 ◽  
Vol 97 (2) ◽  
pp. 114-125 ◽  
Author(s):  
Richa Sharma ◽  
Mukund M.D. Pramanik ◽  
Balasubramanian Chandramouli ◽  
Namrata Rastogi ◽  
Niti Kumar
Keyword(s):  
Protein Folding ◽  
Small Molecules ◽  
Pharmacological Modulation

scholarly journals Management of Hsp90-Dependent Protein Folding by Small Molecules Targeting the Aha1 Co-Chaperone

2020 ◽  
Vol 27 (3) ◽  
pp. 292-305.e6 ◽  
Author(s):  
Jay K. Singh ◽  
Darren M. Hutt ◽  
Bradley Tait ◽  
Naihsuan C. Guy ◽  
Jeffrey C. Sivils ◽  
...  
Keyword(s):  
Protein Folding ◽  
Small Molecules ◽  
Dependent Protein

scholarly journals Chaperoning ribosome assembly

2010 ◽  
Vol 189 (1) ◽  
pp. 11-12 ◽  
Author(s):  
Katrin Karbstein
Keyword(s):  
Protein Folding ◽  
Ribosome Assembly ◽  
Cell Biol ◽  
Nascent Chain ◽  
Cellular Compartments

Chaperones help proteins fold in all cellular compartments, and many associate directly with ribosomes, capturing nascent chains to assist their folding and prevent aggregation. In this issue, new data from Koplin et al. (2010. J. Cell Biol. doi: 10.1083/jcb.200910074) and Albanèse et al. (2010. J. Cell Biol. doi: 10.1083/jcb.201001054) suggest that in addition to promoting protein folding, the chaperones ribosome-associated complex (RAC), nascent chain–associated complex (NAC), and Jjj1 also help in the assembly of ribosomes.

scholarly journals Chemical rescue of mutant proteins in living cells by naturally occurring small molecules

2021 ◽  
Author(s):  
Daniel S. Hassell ◽  
Marc G. Steingesser ◽  
Ashley S. Denney ◽  
Courtney R. Johnson ◽  
Michael A. McMurray
Keyword(s):  
Protein Folding ◽  
Small Molecules ◽  
Protein Function ◽  
Therapeutic Interventions ◽  
Side Chain ◽  
Enzymatic Reactions ◽  
Chemical Rescue ◽  
Naturally Occurring

AbstractIntracellular proteins function in a complex milieu wherein small molecules influence protein folding and act as essential cofactors for enzymatic reactions. Thus protein function depends not only on amino acid sequence but also on the concentrations of such molecules, which are subject to wide variation between organisms, metabolic states, and environmental conditions. We previously found evidence that exogenous guanidine reverses the phenotypes of specific budding yeast septin mutants by binding to a WT septin at the former site of an Arg side chain that was lost during fungal evolution. Here we used a combination of targeted and unbiased approaches to look for other cases of “chemical rescue” by naturally occurring small molecules. We reportin vivorescue of hundreds of yeast mutants representing a variety of genes, including likely examples of Arg or Lys side chain replacement by the guanidinium ion. Failed rescue of targeted mutants highlight features required for rescue, as well as key differences between thein vitroandin vivoenvironments. Some non-Arg mutants rescued by guanidine likely result from “off-target” effects on specific cellular processes in WT cells. Molecules isosteric to guanidine and known to influence protein folding had a range of effects, from essentially none for urea, to rescue of a few mutants by DMSO. Strikingly, the osmolyte trimethylamine-N-oxide rescued ∼20% of the mutants we tested, likely reflecting combinations of direct and indirect effects on mutant protein function. Our findings illustrate the potential of natural small molecules as therapeutic interventions and drivers of evolution.

Chaperone-assisted degradation: multiple paths to destruction

2010 ◽  
Vol 391 (5) ◽  
pp. 481-489 ◽  
Author(s):  
Nadja Kettern ◽  
Michael Dreiseidler ◽  
Riga Tawo ◽  
Jörg Höhfeld
Keyword(s):  
Protein Folding ◽  
Molecular Chaperones ◽  
Mammalian Cells ◽  
Molecular Mechanisms ◽  
Degradation Pathways ◽  
Lysosomal Compartment ◽  
Pharmacological Modulation ◽  
Native Proteins ◽  
Multiple Paths ◽  
Protein Folding And Assembly

Abstract Molecular chaperones are well known as facilitators of protein folding and assembly. However, in recent years multiple chaperone-assisted degradation pathways have also emerged, including CAP (chaperone-assisted proteasomal degradation), CASA (chaperone-assisted selective autophagy), and CMA (chaperone-mediated autophagy). Within these pathways chaperones facilitate the sorting of non-native proteins to the proteasome and the lysosomal compartment for disposal. Impairment of these pathways contributes to the development of cancer, myopathies, and neurodegenerative diseases. Chaperone-assisted degradation thus represents an essential aspect of cellular proteostasis, and its pharmacological modulation holds the promise to ameliorate some of the most devastating diseases of our time. Here, we discuss recent insights into molecular mechanisms underlying chaperone-assisted degradation in mammalian cells and highlight its biomedical relevance.

scholarly journals ATP emerged to induce protein folding, inhibit aggregation and increase stability

2019 ◽  
Author(s):  
Jian Kang ◽  
Liangzhong Lim ◽  
Jianxing Song
Keyword(s):  
Protein Folding ◽  
Small Molecules ◽  
Origin Of Life ◽  
Protein Homeostasis ◽  
Nmr Characterization ◽  
General Capacity ◽  
The Origin Of Life ◽  
First Time ◽  
Control Protein

AbstractBy NMR characterization of effects of ATP and related molecules on the folding and dynamics of the ALS-causing C71G-PFN1 and nascent hSOD1, we reveal for the first time that ATP has a general capacity in inducing protein folding with the highest efficiency known so far. This capacity was further identified to result from triphosphate, a key intermediate in prebiotic chemistry, which, however, can severely trigger protein aggregation. Remarkably, by joining adenosine and triphosphate together, ATP integrates three abilities to simultaneously induce protein folding, inhibit aggregation and increase thermodynamic stability. Our study implies that the emergence of ATP might represent an irreplaceable step essential for the Origin of Life, and decrypts a principle for engineering small molecules with three functions to treat aggregation-associated ageing and diseases.One sentence summaryBy joining adenosine and triphosphate, ATP integrates three abilities to control protein homeostasis for the Origin of Life.

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