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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.)

New insights on human Hsp70-escort protein 1: Chaperone activity, interaction with liposomes, cellular localizations and HSPA's self-assemblies remodeling

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Dores-Silva, Paulo Roberto [1, 2] ; Rodrigues Kiraly, Vanessa Thomaz [1] ; de Oliveira Moritz, Milene Nobrega [1] ; Balasco Serrao, Vitor Hugo [3] ; Siqueira dos Passos, Patricia Maria [4] ; Spagnol, Valentine [4] ; Teixeira, Felipe Roberti [4] ; Gava, Lisandra Marques [4] ; Cauvi, David Mario [2] ; Inacio Ramos, Carlos Henrique [5] ; De Maio, Antonio [6, 7, 2] ; Borges, Julio Cesar [1]
Total Authors: 12
Affiliation:
[1] Univ Sao Paulo, Sao Carlos Inst Chem, Sao Carlos, SP - Brazil
[2] Univ Calif San Diego, Sch Med, Dept Surg, La Jolla, CA 92093 - USA
[3] Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON - Canada
[4] Univ Fed Sao Carlos, Dept Genet & Evolut, Sao Carlos, SP - Brazil
[5] State Univ Campinas UNICAMP, Inst Chem, Campinas, SP - Brazil
[6] Univ Calif San Diego, Sch Med, Dept Neurosci, La Jolla, CA 92093 - USA
[7] Univ Calif San Diego, Ctr Invest Hlth & Educ Dispar, La Jolla, CA 92093 - USA
Total Affiliations: 7
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 182, p. 772-784, JUL 1 2021.
Web of Science Citations: 0
Abstract

The 70 kDa heat shock proteins (Hsp70) are prone to self-assembly under thermal stress conditions, forming supramolecular assemblies (SMA), what may have detrimental consequences for cellular viability. In mitochondria, the cochaperone Hsp70-escort protein 1 (Hep1) maintains mitochondrial Hsp70 (mtHsp70) in a soluble and functional state, contributing to preserving proteostasis. Here we investigated the interaction between human Hep1 (hHep1) and HSPA9 (human mtHsp70) or HSPA1A (Hsp70-1A) in monomeric and thermic SMA states to unveil further information about the involved mechanisms. hHep1 was capable of blocking the formation of HSPA SMAs under a thermic treatment and stimulated HSPA ATPase activity in both monomeric and preformed SMA. The interaction of hHep1 with both monomeric and SMA HSPAs displayed a stoichiometric ratio close to 1, suggesting that hHep1 has access to most protomers within the SMA. Interestingly, hHep1 remodeled HSPA9 and HSPA1A SMAs into smaller forms. Furthermore, hHep1 was detected in the mitochondria and nucleus of cells transfected with the respective coding DNA and interacted with liposomes resembling mitochondrial membranes. Altogether, these new features reinforce that hHep1 act as a \& ldquo;chaperone for a chaperone \& rdquo;, which may play a critical role in cellular proteostasis. (c) 2021 Elsevier B.V. All rights reserved. (AU)

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 type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 14/07206-6 - Studies of the mitochondrial HSP70 of human and protozoa: structural and functional approaches
Grantee:Julio Cesar Borges
Support type: Regular Research Grants
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 type: Research Projects - Thematic Grants
FAPESP's process: 16/25798-3 - Functional consequences of rearrangements to the FBXL17 gene detected in patient samples and cancer cell lines, on the E3 ubiquitin-ligase SCF(Fbxl17) activity
Grantee:Felipe Roberti Teixeira
Support type: Regular Research Grants
FAPESP's process: 09/54216-9 - Acquisition of a 200kV transmission electron microscope for the characterization of nanostructures and biological materials
Grantee:Edson Antonio Ticianelli
Support type: Multi-user Equipment Program
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 type: Research Projects - Thematic Grants
FAPESP's process: 17/07879-9 - Does the protein UXT, which is a required for the NF-kB pathway, a substrate of the E3 ubiquitin-ligase SCF(Fbxo7)?
Grantee:Valentine Spagnol
Support type: Scholarships in Brazil - Scientific Initiation
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 type: Regular Research 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 type: Regular Research Grants
FAPESP's process: 12/23730-1 - Characterization of macromolecular interactions of proteins involved in the selenocysteine synthesis from Escherichia coli
Grantee:Vitor Hugo Balasco Serrão
Support type: Scholarships in Brazil - Doctorate