Unzipping the Secrets of Amyloid Disassembly by the Human Disaggregase
dc.contributor.author | Franco Budia, Aitor | |
dc.contributor.author | Velasco Carneros, Lorea | |
dc.contributor.author | Álvarez Peña, Naiara | |
dc.contributor.author | Orozco, Natalia | |
dc.contributor.author | Moro Pérez, Fernando | |
dc.contributor.author | Prado Ruiz, Adelina | |
dc.contributor.author | Muga Villate, Arturo | |
dc.date.accessioned | 2021-10-26T10:49:57Z | |
dc.date.available | 2021-10-26T10:49:57Z | |
dc.date.issued | 2021-10-14 | |
dc.identifier.citation | Cells 10(10) : (2021) // Article ID 2745 | es_ES |
dc.identifier.issn | 2073-4409 | |
dc.identifier.uri | http://hdl.handle.net/10810/53634 | |
dc.description.abstract | Neurodegenerative diseases (NDs) are increasingly positioned as leading causes of global deaths. The accelerated aging of the population and its strong relationship with neurodegeneration forecast these pathologies as a huge global health problem in the upcoming years. In this scenario, there is an urgent need for understanding the basic molecular mechanisms associated with such diseases. A major molecular hallmark of most NDs is the accumulation of insoluble and toxic protein aggregates, known as amyloids, in extracellular or intracellular deposits. Here, we review the current knowledge on how molecular chaperones, and more specifically a ternary protein complex referred to as the human disaggregase, deals with amyloids. This machinery, composed of the constitutive Hsp70 (Hsc70), the class B J-protein DnaJB1 and the nucleotide exchange factor Apg2 (Hsp110), disassembles amyloids of α-synuclein implicated in Parkinson’s disease as well as of other disease-associated proteins such as tau and huntingtin. We highlight recent studies that have led to the dissection of the mechanism used by this chaperone system to perform its disaggregase activity. We also discuss whether this chaperone-mediated disassembly mechanism could be used to solubilize other amyloidogenic substrates. Finally, we evaluate the implications of the chaperone system in amyloid clearance and associated toxicity, which could be critical for the development of new therapies. | es_ES |
dc.description.sponsorship | This research was funded by MCI/AEI/FEDER, UE (grant PID2019-111068GB-I00) and by the Basque Government (grant IT1201-19). L.V.-C. is the recipient of a predoctoral fellowship from the UPV/EHU and N.O. holds a contract funded by Fundacion Biofisika Bizkaia. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | MDPI | es_ES |
dc.relation | info:eu-repo/grantAgreement/MICINN/PID2019-111068GB-I00 | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | |
dc.subject | neurodegeneration | es_ES |
dc.subject | amyloid | es_ES |
dc.subject | chaperone | es_ES |
dc.subject | disaggregase | es_ES |
dc.title | Unzipping the Secrets of Amyloid Disassembly by the Human Disaggregase | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.date.updated | 2021-10-22T13:55:53Z | |
dc.rights.holder | 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). | es_ES |
dc.relation.publisherversion | https://www.mdpi.com/2073-4409/10/10/2745/htm | es_ES |
dc.identifier.doi | 10.3390/cells10102745 | |
dc.departamentoes | Bioquímica y biología molecular | |
dc.departamentoeu | Biokimika eta biologia molekularra |
Files in this item
This item appears in the following Collection(s)
Except where otherwise noted, this item's license is described as 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).