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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies

Full text
Author(s):
Kiraly, Vanessa T. R. [1] ; Dores-Silva, Paulo R. [1, 2] ; Serrao, Vitor H. B. [3] ; Cauvi, David M. [2] ; De Maio, Antonio [2, 4, 5] ; Borges, Julio C. [1]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Sao Carlos Inst Chem, Sao Carlos, SP - Brazil
[2] Univ Calif, Sch Med, Dept Surg, La Jolla, CA - USA
[3] Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON - Canada
[4] Univ Calif San Diego, Ctr Invest Hlth & Educ Dispar, La Jolla, CA 92093 - USA
[5] Univ Calif, Sch Med, Dept Neurosci, La Jolla, CA - USA
Total Affiliations: 5
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 146, p. 320-331, MAR 1 2020.
Web of Science Citations: 0
Abstract

The Hsp70 family of heat shock proteins plays a critical function in maintaining cellular homeostasis within various subcellular compartments. The human mitochondrial Hsp70 (HSPA9) has been associated with cellular death, senescence, cancer and neurodegenerative diseases, which is the rational for the name mortalin. It is well documented that mortalin, such as other Hsp70s, is prone to self-aggregation, which is related to mitochondria biogenesis failure. Here, we investigated the assembly, structure and function of thermic aggregates/oligomers of recombinant human mortalin and Hsp70-1A (HSPA1A). Summarily, both Hsp70 thermic aggregates have characteristics of supramolecular assemblies. They display characteristic organized structures and partial ATPase activity, despite their nanometric size. Indeed, we observed that the interaction of these aggregates/oligomers with liposomes is similar to monomeric Hsp70s and, finally, they were non-toxic over neuroblastoma cells. These findings revealed that high molecular mass oligomers of mortalin and Hsp70-1A preserved some of the fundamental functions of these proteins. (C) 2019 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 17/26131-5 - The chaperome: study of the relationship of the structure of its components and the maintenance of proteostasis
Grantee:Carlos Henrique Inacio Ramos
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 14/07206-6 - Studies of the mitochondrial HSP70 of human and protozoa: structural and functional approaches
Grantee:Julio Cesar Borges
Support Opportunities: Regular Research Grants
FAPESP's process: 11/23110-0 - Using isothermal titration calorimetry for the determination of thermodynamic properties of protein-ligand and protein-protein interactions
Grantee:Julio Cesar Borges
Support Opportunities: Regular Research Grants
FAPESP's process: 12/50161-8 - Study of the structure and function of the Hsp90 chaperone with emphasis on its role in cellular homeostasis
Grantee:Carlos Henrique Inacio Ramos
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 17/07335-9 - Studies of human HSP70 isoforms residing in the cytoplasm and mitochondria and their high molecular weight oligomers: interaction with co-chaperones and client proteins
Grantee:Julio Cesar Borges
Support Opportunities: Regular Research Grants
FAPESP's process: 14/16646-0 - Human mortalin: interaction with co-chaperones, p53 and mutants, aggregation kinectics, regulation/modulation and vesicle secretion
Grantee:Paulo Roberto das Dores da Silva
Support Opportunities: Scholarships in Brazil - Post-Doctoral