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Structural studies on the assembly of septin complexes by transmission electron microscopy and single particle analysis

Grant number: 18/20209-5
Support type:Scholarships in Brazil - Doctorate
Effective date (Start): January 01, 2019
Effective date (End): February 28, 2021
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal Investigator:Richard Charles Garratt
Grantee:Deborah Cezar Mendonça
Home Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil

Abstract

Septins are cytoskeletal GTPases involved in a number of important intracellular processes including cell division, vesicle trafficking, exocytosis, among others. In addition, their role in the formation of barriers which prevent the free diffusion of plasma membrane components has also been reported. In humans, changes in the expression levels of septins are related to several types of Cancer and mutations in some amino acids are also related to male infertility and temperature-sensitive phenotypes in yeast. They are also found in protein clusters in the brain of patients with neurological diseases such as Alzheimer's and Parkinson's. Septins are capable of polymerizing in the form of heterocomplexes resulting in filaments that subsequently organize into higher order structures. However, there are many mechanical aspects of these proteins that are not fully understood, including how heterocomplexes cluster correctly. This study aims to analyze the septins complexes that have not yet been studied in structural terms using electron transmission electron microscopy and isolated particle analysis, contributing to a better understanding of the mechanism of polymerization and self-assembly of these proteins. (AU)