Interplay between protein homeostasis networks in protein aggregation and proteotoxicity
Open Access
- 18 September 2009
- journal article
- review article
- Published by Wiley in Peptide Science
- Vol. 93 (3), 229-236
- https://doi.org/10.1002/bip.21304
Abstract
The misfolding and aggregation of disease proteins is characteristic of numerous neurodegenerative diseases. Particular neuronal populations are more vulnerable to proteotoxicity while others are more apt to tolerate the misfolding and aggregation of disease proteins. Thus, the cellular environment must play a significant role in determining whether disease proteins are converted into toxic or benign forms. The endomembrane network of eukaryotes divides the cell into different subcellular compartments that possess distinct sets of molecular chaperones and protein interaction networks. Chaperones act as agonists and antagonists of disease protein aggregation to prevent the accumulation of toxic intermediates in the aggregation pathway. Interacting partners can also modulate the conformation and localization of disease proteins and thereby influence proteotoxicity. Thus, interplay between these protein homeostasis network components can modulate the self‐association of disease proteins and determine whether they elicit a toxic or benign outcome. © 2009 Wiley Periodicals, Inc. Biopolymers 93: 229–236, 2010. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.comThis publication has 103 references indexed in Scilit:
- Rethinking ALS: The FUS about TDP-43Cell, 2009
- Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prionsThe EMBO Journal, 2008
- The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactionsNature, 2006
- Chaperonin TRiC Promotes the Assembly of polyQ Expansion Proteins into Nontoxic OligomersMolecular Cell, 2006
- The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperonesCellular and Molecular Life Sciences, 2006
- Destruction or Potentiation of Different Prions Catalyzed by Similar Hsp104 Remodeling ActivitiesMolecular Cell, 2006
- Molecular Chaperones and Protein Quality ControlCell, 2006
- Structure of the cross-β spine of amyloid-like fibrilsNature, 2005
- Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal deathNature, 2004
- Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's DiseaseBiochemistry, 2001