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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.)

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

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Author(s):
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]
Total Authors: 9
Affiliation:
[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
Total Affiliations: 6
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 133, p. 428-435, JUL 15 2019.
Web of Science Citations: 0
Abstract

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)

FAPESP's process: 14/15546-1 - Septins: comparative studies and the correlation between structure and function
Grantee:Richard Charles Garratt
Support type: Research Projects - Thematic Grants
FAPESP's process: 17/07709-6 - Use of low resolution techniques for structural analysis of septin filaments
Grantee:Patricia Suemy Kumagai
Support type: Scholarships in Brazil - Post-Doctorate