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Use of low resolution techniques for structural analysis of septin filaments

Grant number: 17/07709-6
Support Opportunities:Scholarships in Brazil - Post-Doctoral
Effective date (Start): July 01, 2017
Effective date (End): September 30, 2019
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal Investigator:Ana Paula Ulian de Araujo
Grantee:Patricia Suemy Kumagai
Host Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
Associated research grant:14/15546-1 - Septins: comparative studies and the correlation between structure and function, AP.TEM


The importance of septins in several processes in eukaryotes is evident and represents one of the main reasons for the study of these proteins. Thus, structural and functional characterization studies of this family are essential to clarify these aspects, as well as to the understanding of the function of these proteins in the several pathologies to which they have been related. In this context, the objective of this proposal is the extension of the structural analyzes of individual septins to protein complexes and is inserted in the context of the Thematic project. In humans, 13 genes of septins are found, and the number of proteins encoded by them may be much higher because of the existence of alternative splicing, thus considerably increasing the number of expressed isoforms, some of which are tissue-specific. Given the large number of theoretical possibilities of complexes, one of the major challenges today is to understand the spontaneous assembly of heterofilaments and specifically how each septin recognizes its correct partners through the G and NC interfaces. Thus, this project aims to explore in structural terms the various combinations of human septins in heterocomplexes, addressing low resolution techniques.

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
LEONARDO, DIEGO A.; CAVINI, ITALO A.; SALA, FERNANDA A.; MENDONCA, DEBORAH C.; ROSA, HIGOR V. D.; KUMAGAI, PATRICIA S.; CRUSCA JR, EDSON; VALADARES, NAPOLEAO F.; MARQUES, IVO A.; BRANDAO-NETO, JOSE; et al. Orientational Ambiguity in Septin Coiled Coils and its Structural Basis. Journal of Molecular Biology, v. 433, n. 9, . (18/20209-5, 16/04658-9, 17/07709-6, 19/22000-9, 14/15546-1, 15/00062-1, 13/04433-9, 15/16811-3, 18/19992-7)
KUMAGAI, PATRICIA S.; MARTINS, CARLA S.; SALES, ELISA M.; ROSA, HIGOR V. D.; MENDONCA, DEBORAH C.; DAMALIO, JULIO CESAR P.; SPINOZZI, FRANCESCO; ITRI, ROSANGELA; ARAUJO, ANA PAULA U.. Correct partner makes the difference: Septin G-interface plays a critical role in amyloid formation. International Journal of Biological Macromolecules, v. 133, p. 428-435, . (14/15546-1, 17/07709-6)

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