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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.)

Biophysical dissection of schistosome septins: Insights into oligomerization and membrane binding

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Author(s):
Zeraik, Ana Eliza ; Staykova, Margarita ; Fontes, Marina Gabriel ; Nemuraite, Indre ; Quinlan, Roy ; Ulian Araujo, Ana Paula ; DeMarco, Ricardo
Total Authors: 7
Document type: Journal article
Source: Biochimie; v. 131, p. 96-105, DEC 2016.
Web of Science Citations: 2
Abstract

Septins are GTP-binding proteins that are highly conserved among eukaryotes and which are usually membrane-associated. They have been linked to several critical cellular functions such as exocytosis and ciliogenesis, but little mechanistic detail is known. Their assembly into filaments and membrane binding properties are incompletely understood and that is specially so for non-human septins where such information would offer therapeutic potential. In this study we use Schistosoma mansoni, exhibiting just four septin genes, as a simpler model for characterizing the septin structure and organization. We show that the biochemical and biophysical proprieties of its SmSEPT5 and SmSEPT10 septins are consistent with their human counterparts of subgroups SEPT2 and SEPT6, respectively. By succeeding to isolate stable constructs comprising distinct domains of SmSEPT5 and SmSEPT10 we were able to infer the influence of terminal interfaces in the oligomerization and membrane binding properties. For example, both proteins tended to form oligomers interacting by the N- and C-terminal interfaces in a nucleotide independent fashion but form heterodimers via the G interface, which are nucleotide dependent. Furthermore, we report for the first time that it is the C-terminus of SmSETP10, rather than the N-terminal polybasic region found in other septins, that mediates its binding to liposomes. Upon binding we observe formation of discrete lipo-protein clusters and higher order septin structures, making our system an exciting model to study interactions of septins with biological membranes. (C) 2016 Elsevier B.V. and Socifte Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. (AU)

FAPESP's process: 13/20715-4 - Studies of the correlation between septin dynamics and Ca2+ homeostasis in muscular cells from Schistosoma mansoni
Grantee:Ana Eliza Zeraik
Support type: Scholarships in Brazil - Post-Doctorate
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