Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity

Mohyeddine Omrane; Amanda Souza Camara; Cyntia Taveneau; Nassima Benzoubir; Thibault Tubiana; Jinchao Yu; Raphaël Guérois; Didier Samuel; Bruno Goud; Christian Poüs; Stéphane Bressanelli; Richard Charles Garratt; Abdou Rachid Thiam; Ama Gassama-Diagne

doi:10.1016/j.isci.2019.02.015

Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity

Mohyeddine Omrane, Amanda Souza Camara, Cyntia Taveneau, Nassima Benzoubir, Thibault Tubiana, Jinchao Yu, Raphaël Guérois, Didier Samuel, Bruno Goud, Christian Poüs, Stéphane Bressanelli, Richard Charles Garratt, Abdou Rachid Thiam, Ama Gassama-Diagne

Research output: Contribution to journal › Article › Research › peer-review

29 Citations (Scopus)

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.

Original language	English
Pages (from-to)	138-153
Number of pages	16
Journal	iScience
Volume	13
DOIs	https://doi.org/10.1016/j.isci.2019.02.015
Publication status	Published - 29 Mar 2019
Externally published	Yes

Keywords

Cell Biology
Functional Aspects of Cell Biology
Membrane Architecture
Molecular Interaction

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10.1016/j.isci.2019.02.015

290235469-oaFinal published version, 8.34 MB

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title = "Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity",

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.",

keywords = "Cell Biology, Functional Aspects of Cell Biology, Membrane Architecture, Molecular Interaction",

author = "Mohyeddine Omrane and Camara, {Amanda Souza} and Cyntia Taveneau and Nassima Benzoubir and Thibault Tubiana and Jinchao Yu and Rapha{\"e}l Gu{\'e}rois and Didier Samuel and Bruno Goud and Christian Po{\"u}s and St{\'e}phane Bressanelli and Garratt, {Richard Charles} and Thiam, {Abdou Rachid} and Ama Gassama-Diagne",

year = "2019",

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day = "29",

doi = "10.1016/j.isci.2019.02.015",

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AU - Omrane, Mohyeddine

AU - Camara, Amanda Souza

AU - Taveneau, Cyntia

AU - Benzoubir, Nassima

AU - Tubiana, Thibault

AU - Yu, Jinchao

AU - Guérois, Raphaël

AU - Samuel, Didier

AU - Goud, Bruno

AU - Poüs, Christian

AU - Bressanelli, Stéphane

AU - Garratt, Richard Charles

AU - Thiam, Abdou Rachid

AU - Gassama-Diagne, Ama

PY - 2019/3/29

Y1 - 2019/3/29

N2 - 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.

AB - 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.

KW - Cell Biology

KW - Functional Aspects of Cell Biology

KW - Membrane Architecture

KW - Molecular Interaction

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DO - 10.1016/j.isci.2019.02.015

M3 - Article

AN - SCOPUS:85065305734

SN - 2589-0042

VL - 13

SP - 138

EP - 153

JO - iScience

JF - iScience

ER -

Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity

Abstract

Keywords

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Other files and links

Erratum: Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity (iScience (2019) 13 (138–153), (S2589004219300495), (10.1016/j.isci.2019.02.015))

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