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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Correct partner makes the difference: Septin G-interface plays a critical role in amyloid formation

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Autor(es):
Kumagai, Patricia S. [1] ; Martins, Carla S. [1, 2] ; Sales, Elisa M. [3, 4] ; Rosa, Higor V. D. [1] ; Mendonca, Deborah C. [1] ; Damalio, Julio Cesar P. [5] ; Spinozzi, Francesco [6] ; Itri, Rosangela [3] ; Araujo, Ana Paula U. [1]
Número total de Autores: 9
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Inst Fis Sao Carlos, Ave Joao Dagnone 1100, BR-13563120 Sao Carlos, SP - Brazil
[2] Inst Fresnel, Marseille - France
[3] Univ Sao Paulo, Inst Fis, Rua Matao 1371, BR-05508090 Sao Paulo, SP - Brazil
[4] IPT Inst Technol Res, Ave Prof Almeida Prado 532, BR-05508280 Sao Paulo, SP - Brazil
[5] Inst Fed Educ & Tecnol Sao Paulo, Campus Avare, BR-18707150 Avare, SP - Brazil
[6] Polytech Univ Marche, Dept Life & Environm Sci, Via Brecce Bianche, I-60131 Ancona - Italy
Número total de Afiliações: 6
Tipo de documento: Artigo Científico
Fonte: International Journal of Biological Macromolecules; v. 133, p. 428-435, JUL 15 2019.
Citações Web of Science: 0
Resumo

Septins are members of a group of GTP-binding proteins highly conserved in eukaryotes, being linked to diverse cell processes, such as cytokinesis and membrane association. On the other hand, the malfunction of septins is linked to several pathological processes including neurodegeneration and oncogenesis. Septins interact with each other forming heterocomplexes that polymerize in filaments. Two types of interface between septins alternate along the filament: the G-interface (involving the GTP binding sites), and the NC-interface. This work focuses on the physiological G-interface of SEPT2, used in the SEPT6G-SEPT2G heterodimer assembly, to verify the impact of this interaction on the thermostability and amyloid formation. We found that the SEPT6GSEPT2G moves to an irreversible state with the ability to bind thioflavin-T at high temperatures, suggesting its amyloid-like nature. Noteworthy, this takes place at a higher temperature than the one observed to the single septins, showing greater thermal/structural stability. Taken together, our results show that in the absence of the partners, the septin becomes unstable and susceptible to amyloid aggregation/formation even in physiological temperatures, and the G-interface appears to have a critical role in this process. (C) 2019 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 14/15546-1 - Septinas: estudos comparativos visando correlacionar estrutura e função
Beneficiário:Richard Charles Garratt
Linha de fomento: Auxílio à Pesquisa - Temático
Processo FAPESP: 17/07709-6 - Utilização de técnicas de baixa resolução para análises estruturais de filamentos de septinas
Beneficiário:Patricia Suemy Kumagai
Linha de fomento: Bolsas no Brasil - Pós-Doutorado