Septin 4 : complexes and interactions

• Grant number: 12/22717-1
• Support Opportunities: Scholarships in Brazil - Doctorate
• Start date: June 01, 2013
• End date: May 31, 2015
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: Richard Charles Garratt
• Grantee: Nayara Cavalcante Silva
• Host Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil

Abstract

Septins are nucleotide binding proteins organized in filaments similar with cytoskeletal proteins. Their main function seems to be related with cell compartmentalization and cell polarization, which is crucial for certain cell types such as spermatozoids, cilia cells and neurons and in all those cell types the expression have been detected. Septins are organized in filaments which can assume diverse shapes. Also are conserved proteins in metazoans and filaments composition is quite diverse, until now is not well known which control the composition and arrangements of different filaments. Humans express 13 septins that are divided in four different groups and Kinoshita has proposed that filaments are composed by one septin from which group. It is not known the real function to GTP hydrolysis, maybe the conformational change generate new interaction sites and possibly facilitate filament formation. It is known only few septins interaction proteins then the main focus of that project will be investigate septins interaction partners more focused to septin 4 and how those interactions could change the biology of septin 4. One of those interactions is Alfa sunuclein, we would like to determine the interaction region. Another interest will be determining the structures of the complexes in which septin 4 take place by X-ray diffraction and/or electron microscopy.