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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

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Autor(es):
Zeraik, Ana Eliza ; Staykova, Margarita ; Fontes, Marina Gabriel ; Nemuraite, Indre ; Quinlan, Roy ; Ulian Araujo, Ana Paula ; DeMarco, Ricardo
Número total de Autores: 7
Tipo de documento: Artigo Científico
Fonte: Biochimie; v. 131, p. 96-105, DEC 2016.
Citações Web of Science: 2
Resumo

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)

Processo FAPESP: 13/20715-4 - Estudo da correlação entre a dinâmica de septinas e a homeostase de Ca2+ em células musculares de Schistosoma mansoni
Beneficiário:Ana Eliza Zeraik
Linha de fomento: Bolsas no Brasil - Pós-Doutorado
Processo FAPESP: 14/15546-1 - Septinas: estudos comparativos visando correlacionar estrutura e função
Beneficiário:Richard Charles Garratt
Linha de fomento: Auxílio à Pesquisa - Temático