Abstract – Publication

Septin 9 has two polybasic domains critical to septin filament assembly and golgi integrity.
OMRANE, Mohyeddine; CAMARA, Amanda Souza; TAVENEAU, Cyntia; BENZOUBIR, Nassima; TUBIANA, Thibault; YU, Jinchao; GUÉROIS, Raphaël; SAMUEL, Didier; GOUD, Bruno; POÜS, Christian; BRESSANELLI, Stéphane; GARRATT, Richard Charles; THIAM, Abdou Rachid; GASSAMA-DIAGNE, Ama.
Abstract: Septins are GTP-binding proteins involved in several membrane remodeling mechanisms. They associate with membranes, presumably using a polybasic domain (PB1) that interacts with phosphoinositides (PIs). Membrane-bound septins assemble into microscopic structures that regulate membrane shape. How septins interact with PIs and then assemble and shape membranes is poorly understood. Here, we found that septin 9 has a second polybasic domain (PB2) conserved in the human septin family. Similar to PB1, PB2 binds specifically to PIs, and both domains are critical for septin filament formation. However, septin 9 membrane association is not dependent on these PB domains, but on putative PB-adjacent amphipathic helices. The presence of PB domains guarantees protein enrichment in PI-contained membranes, which is critical for PI-enriched organelles. In particular, we found that septin 9 PB domains control the assembly and functionality of the Golgi apparatus. Our findings offer further insight into the role of septins in organelle morphology.
IScience
v. 13, p. 138-153 - Ano: 2019
http://dx.doi.org/10.1016/j.isci.2019.02.015
    @article={002939636,author = {OMRANE, Mohyeddine; CAMARA, Amanda Souza; TAVENEAU, Cyntia; BENZOUBIR, Nassima; TUBIANA, Thibault; YU, Jinchao; GUÉROIS, Raphaël; SAMUEL, Didier; GOUD, Bruno; POÜS, Christian; BRESSANELLI, Stéphane; GARRATT, Richard Charles; THIAM, Abdou Rachid; GASSAMA-DIAGNE, Ama.},title={Septin 9 has two polybasic domains critical to septin filament assembly and golgi integrity},journal={IScience},note={v. 13, p. 138-153},year={2019}}

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