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Article ; Online: Mlg1, a yeast acyltransferase located in ER membranes associated with mitochondria (MAMs), is involved in de novo synthesis and remodelling of phospholipids.

Laquel, Patricia / Ayciriex, Sophie / Doignon, François / Camougrand, Nadine / Fougère, Louise / Rocher, Christophe / Wattelet-Boyer, Valérie / Bessoule, Jean-Jacques / Testet, Eric

The FEBS journal

2024

Abstract: In cells, phospholipids contain acyl chains of variable lengths and saturation, features that affect their functions. Their de novo synthesis in the endoplasmic reticulum takes place via the cytidine diphosphate diacylglycerol (CDP-DAG) and Kennedy ... ...

Abstract	In cells, phospholipids contain acyl chains of variable lengths and saturation, features that affect their functions. Their de novo synthesis in the endoplasmic reticulum takes place via the cytidine diphosphate diacylglycerol (CDP-DAG) and Kennedy pathways, which are conserved in eukaryotes. PA is a key intermediate for all phospholipids (PI, PIPs, PS, PE, PC, PG and CL). The de novo synthesis of PA occurs by acylation of glycerophosphate leading to the synthesis of 1-acyl lysoPA and subsequent acylation of 1-acyl lysoPA at the sn-2 position. Using membranes from Escherichia coli overexpressing MLG1, we showed that the yeast gene MLG1 encodes an acyltransferase, leading specifically to the synthesis of PA from 1-acyl lysoPA. Moreover, after their de novo synthesis, phospholipids can be remodelled by acyl exchange with one and/or two acyl chains exchanged at the sn-1 and/or sn-2 position. Based on shotgun lipidomics of the reference and mlg1Δ strains, as well as biochemical assays for acyltransferase activities, we identified an additional remodelling activity for Mlg1p, namely, incorporation of palmitic acid into the sn-1 position of PS and PE. By using confocal microscopy and subcellular fractionation, we also found that this acyltransferase is located in ER membranes associated with mitochondria, a finding that highlights the importance of these organelles in the global cellular metabolism of lipids.
Language	English
Publishing date	2024-01-31
Publishing country	England
Document type	Journal Article
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.17068
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Article ; Online: Phosphoinositides containing stearic acid are required for interaction between Rho GTPases and the exocyst to control the late steps of polarized exocytosis.

Laquel, Patricia / Testet, Eric / Tuphile, Karine / Cullin, Christophe / Fouillen, Laetitia / Bessoule, Jean-Jacques / Doignon, François

Traffic (Copenhagen, Denmark)

2022 Volume 23, Issue 2, Page(s) 120–136

Abstract: Cell polarity is achieved by regulators such as small G proteins, exocyst members and phosphoinositides, with the latter playing a key role when bound to the exocyst proteins Sec3p and Exo70p, and Rho GTPases. This ensures asymmetric growth via the ... ...

Abstract	Cell polarity is achieved by regulators such as small G proteins, exocyst members and phosphoinositides, with the latter playing a key role when bound to the exocyst proteins Sec3p and Exo70p, and Rho GTPases. This ensures asymmetric growth via the routing of proteins and lipids to the cell surface using actin cables. Previously, using a yeast mutant for a lysophosphatidylinositol acyl transferase encoded by the PSI1 gene, we demonstrated the role of stearic acid in the acyl chain of phosphoinositides in cytoskeletal organization and secretion. Here, we use a genetic approach to characterize the effect on late steps of the secretory pathway. The constitutive overexpression of PSI1 in mutants affecting kinases involved in the phosphoinositide pathway demonstrated the role of molecular species containing stearic acid in bypassing a lack of phosphatidylinositol-4-phosphate (PI(4)P) at the plasma membrane, which is essential for the function of the Cdc42p module. Decreasing the levels of stearic acid-containing phosphoinositides modifies the environment of the actors involved in the control of late steps in the secretory pathway. This leads to decreased interactions between Exo70p and Sec3p, with Cdc42p, Rho1p and Rho3p, because of disruption of the GTP/GDP ratio of at least Rho1p and Rho3p GTPases, thereby preventing activation of the exocyst.
MeSH term(s)	Exocytosis/physiology ; Phosphatidylinositols/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Stearic Acids ; Vesicular Transport Proteins/metabolism ; rho GTP-Binding Proteins/genetics
Chemical Substances	Phosphatidylinositols ; Saccharomyces cerevisiae Proteins ; Stearic Acids ; Vesicular Transport Proteins ; stearic acid (4ELV7Z65AP) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-01-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12829
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Article ; Online: Requirement of Phosphoinositides Containing Stearic Acid To Control Cell Polarity

Doignon, François / Laquel, Patricia / Testet, Eric / Tuphile, Karine / Fouillen, Laetitia / Bessoule, Jean-Jacques

Molecular and Cellular Biology. 2016 Mar. 1, v. 36, no. 5 p.765-780

2016

Abstract: Phosphoinositides (PIPs) are present in very small amounts but are essential for cell signaling, morphogenesis, and polarity. By mass spectrometry, we demonstrated that some PIPs with stearic acyl chains were strongly disturbed in a psi1Δ Saccharomyces ... ...

Abstract	Phosphoinositides (PIPs) are present in very small amounts but are essential for cell signaling, morphogenesis, and polarity. By mass spectrometry, we demonstrated that some PIPs with stearic acyl chains were strongly disturbed in a psi1Δ Saccharomyces cerevisiae yeast strain deficient in the specific incorporation of a stearoyl chain at the sn-1 position of phosphatidylinositol. The absence of PIPs containing stearic acid induced disturbances in intracellular trafficking, although the total amount of PIPs was not diminished. Changes in PIPs also induced alterations in the budding pattern and defects in actin cytoskeleton organization (cables and patches). Moreover, when the PSI1 gene was impaired, a high proportion of cells with bipolar cortical actin patches that occurred concomitantly with the bipolar localization of Cdc42p was specifically found among diploid cells. This bipolar cortical actin phenotype, never previously described, was also detected in a bud9Δ/bud9Δ strain. Very interestingly, overexpression of PSI1 reversed this phenotype.
Keywords	Saccharomyces cerevisiae ; actin ; cell polarity ; diploidy ; genes ; mass spectrometry ; microfilaments ; morphogenesis ; phenotype ; stearic acid ; yeasts
Language	English
Dates of publication	2016-0301
Size	p. 765-780.
Publishing place	Taylor & Francis
Document type	Article ; Online
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00843-15
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Article ; Online: Assignment of

Martinez, Denis / Prouzet-Mauléon, Valérie / Hugues, Michel / Doignon, François / Odaert, Benoît

Biomolecular NMR assignments

2017 Volume 12, Issue 1, Page(s) 129–132

Abstract: The protein Rgd1 is involved in the regulation of cytoskeleton formation and in signalling pathways that control cell polarity and growth in Saccharomyces cerevisiae. Rgd1p is composed of a F-BAR domain required for membrane binding and a RhoGAP domain ... ...

Abstract	The protein Rgd1 is involved in the regulation of cytoskeleton formation and in signalling pathways that control cell polarity and growth in Saccharomyces cerevisiae. Rgd1p is composed of a F-BAR domain required for membrane binding and a RhoGAP domain responsible for activating Rho3p and Rho4p, two GTPases respectively involved in bud growth and cytokinesis. Rgd1p is recruited to the membrane through interactions with phosphoinositide lipids, which bind the two isolated domains and stimulate the RhoGAP activity on Rho4p. As previously shown by crystallography, the membrane-binding F-BAR domain contains a conserved inositol phosphate binding site, which explains the preferential binding of phosphoinositides. In contrast, RhoGAP domains are not expected to bind lipids. In order to unravel this puzzling feature, we solved the three-dimensional structure of the isolated protein and found a cryptic phosphoinositide binding site involving non conserved residues (Martinez et al. 2017). The assignment of the resonances and secondary structure of Rgd1-RhoGAP (aa 450-666) is presented here.
MeSH term(s)	GTPase-Activating Proteins/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Domains ; Protein Structure, Secondary ; Saccharomyces cerevisiae Proteins/chemistry
Chemical Substances	GTPase-Activating Proteins ; RGD1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; rho GTPase-activating protein
Language	English
Publishing date	2017-12-26
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2388861-1
ISSN	1874-270X ; 1874-2718
ISSN (online)	1874-270X
ISSN	1874-2718
DOI	10.1007/s12104-017-9794-z
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Article ; Online: Requirement of Phosphoinositides Containing Stearic Acid To Control Cell Polarity.

Doignon, François / Laquel, Patricia / Testet, Eric / Tuphile, Karine / Fouillen, Laetitia / Bessoule, Jean-Jacques

Molecular and cellular biology

2015 Volume 36, Issue 5, Page(s) 765–780

Abstract	Phosphoinositides (PIPs) are present in very small amounts but are essential for cell signaling, morphogenesis, and polarity. By mass spectrometry, we demonstrated that some PIPs with stearic acyl chains were strongly disturbed in a psi1Δ Saccharomyces cerevisiae yeast strain deficient in the specific incorporation of a stearoyl chain at the sn-1 position of phosphatidylinositol. The absence of PIPs containing stearic acid induced disturbances in intracellular trafficking, although the total amount of PIPs was not diminished. Changes in PIPs also induced alterations in the budding pattern and defects in actin cytoskeleton organization (cables and patches). Moreover, when the PSI1 gene was impaired, a high proportion of cells with bipolar cortical actin patches that occurred concomitantly with the bipolar localization of Cdc42p was specifically found among diploid cells. This bipolar cortical actin phenotype, never previously described, was also detected in a bud9Δ/bud9Δ strain. Very interestingly, overexpression of PSI1 reversed this phenotype.
MeSH term(s)	Actins/metabolism ; Actins/ultrastructure ; Acyltransferases/genetics ; Acyltransferases/metabolism ; Cell Polarity ; Gene Deletion ; Phosphatidylinositols/chemistry ; Phosphatidylinositols/genetics ; Phosphatidylinositols/metabolism ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Stearic Acids/analysis ; Stearic Acids/metabolism
Chemical Substances	Actins ; Phosphatidylinositols ; Saccharomyces cerevisiae Proteins ; Stearic Acids ; stearic acid (4ELV7Z65AP) ; Acyltransferases (EC 2.3.-) ; Cst26 protein, S cerevisiae (EC 2.3.-)
Language	English
Publishing date	2015-12-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00843-15
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Zs.A 1666: Show issues

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Article: Secretory Pathway-Dependent Localization of the Saccharomyces cerevisiae Rho GTPase-Activating Protein Rgd1p at Growth Sites

Lefèbvre, Fabien / Prouzet-Mauléon, Valérie / Hugues, Michel / Crouzet, Marc / Vieillemard, Aurélie / McCusker, Derek / Thoraval, Didier / Doignon, François

Eukaryotic cell. 2012 May, v. 11, no. 5

2012

Abstract: Establishment and maintenance of cell polarity in eukaryotes depends upon the regulation of Rho GTPases. In Saccharomyces cerevisiae, the Rho GTPase activating protein (RhoGAP) Rgd1p stimulates the GTPase activities of Rho3p and Rho4p, which are involved ...

Abstract	Establishment and maintenance of cell polarity in eukaryotes depends upon the regulation of Rho GTPases. In Saccharomyces cerevisiae, the Rho GTPase activating protein (RhoGAP) Rgd1p stimulates the GTPase activities of Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. Consistent with the distribution of Rho3p and Rho4p, Rgd1p is found mostly in areas of polarized growth during cell cycle progression. Rgd1p was mislocalized in mutants specifically altered for Golgi apparatus-based phosphatidylinositol 4-P [PtdIns(4)P] synthesis and for PtdIns(4,5)P2 production at the plasma membrane. Analysis of Rgd1p distribution in different membrane-trafficking mutants suggested that Rgd1p was delivered to growth sites via the secretory pathway. Rgd1p may associate with post-Golgi vesicles by binding to PtdIns(4)P and then be transported by secretory vesicles to the plasma membrane. In agreement, we show that Rgd1p coimmunoprecipitated and localized with markers specific to secretory vesicles and cofractionated with a plasma membrane marker. Moreover, in vivo imaging revealed that Rgd1p was transported in an anterograde manner from the mother cell to the daughter cell in a vectoral manner. Our data indicate that secretory vesicles are involved in the delivery of RhoGAP Rgd1p to the bud tip and bud neck.
Keywords	GTPase-activating proteins ; Saccharomyces cerevisiae ; cell polarity ; cytokinesis ; eukaryotic cells ; guanosinetriphosphatase ; image analysis ; mutants ; plasma membrane ; secretory granules
Language	English
Dates of publication	2012-05
Size	p. 590-600.
Publishing place	American Society for Microbiology
Document type	Article
ZDB-ID	2077635-4
ISSN	1535-9786 ; 1535-9778
ISSN (online)	1535-9786
ISSN	1535-9778
DOI	10.1128/EC.00042-12
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 5779: Show issues

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Article ; Online: Structural evidence of a phosphoinositide-binding site in the Rgd1-RhoGAP domain.

Martinez, Denis / Langlois d'Estaintot, Béatrice / Granier, Thierry / Tolchard, James / Courrèges, Cécile / Prouzet-Mauléon, Valérie / Hugues, Michel / Gallois, Bernard / Doignon, François / Odaert, Benoît

The Biochemical journal

2017 Volume 474, Issue 19, Page(s) 3307–3319

Abstract: Phosphoinositide lipids recruit proteins to the plasma membrane involved in the regulation of cytoskeleton organization and in signalling pathways that control cell polarity and growth. Among those, Rgd1p is a yeast GTPase-activating protein (GAP) ... ...

Abstract	Phosphoinositide lipids recruit proteins to the plasma membrane involved in the regulation of cytoskeleton organization and in signalling pathways that control cell polarity and growth. Among those, Rgd1p is a yeast GTPase-activating protein (GAP) specific for Rho3p and Rho4p GTPases, which control actin polymerization and stress signalling pathways. Phosphoinositides not only bind Rgd1p, but also stimulate its GAP activity on the membrane-anchored form of Rho4p. Both F-BAR (F-BAR FCH, and BAR) and RhoGAP domains of Rgd1p are involved in lipid interactions. In the Rgd1p-F-BAR domain, a phosphoinositide-binding site has been recently characterized. We report here the X-ray structure of the Rgd1p-RhoGAP domain, identify by NMR spectroscopy and confirm by docking simulations, a new but cryptic phosphoinositide-binding site, comprising contiguous A1, A1' and B helices. The addition of helix A1', unusual among RhoGAP domains, seems to be crucial for lipid interactions. Such a site was totally unexpected inside a RhoGAP domain, as it was not predicted from either the protein sequence or its three-dimensional structure. Phosphoinositide-binding sites in RhoGAP domains have been reported to correspond to polybasic regions, which are located at the unstructured flexible termini of proteins. Solid-state NMR spectroscopy experiments confirm the membrane interaction of the Rgd1p-RhoGAP domain upon the addition of PtdIns(4,5)P
MeSH term(s)	Amino Acid Sequence ; Binding Sites ; Cell Membrane/metabolism ; Crystallography, X-Ray ; GTPase-Activating Proteins/chemistry ; GTPase-Activating Proteins/metabolism ; Liposomes/metabolism ; Magnetic Resonance Spectroscopy ; Models, Biological ; Molecular Docking Simulation ; Phosphatidylinositols/chemistry ; Phosphatidylinositols/metabolism ; Protein Domains ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	GTPase-Activating Proteins ; Liposomes ; Phosphatidylinositols ; RGD1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; rho GTPase-activating protein
Language	English
Publishing date	2017-09-20
Publishing country	England
Document type	Journal Article
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20170331
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Article: Evidence for functional links between the Rgd1-Rho3 RhoGAP-GTPase module and Tos2, a protein involved in polarized growth in Saccharomyces cerevisiae

Claret, Sandra / Roumanie, Olivier / Prouzet-Mauleon, Valérie / Lefebvre, Fabien / Thoraval, Didier / Crouzet, Marc / Doignon, François

FEMS yeast research. 2011 Mar., v. 11, no. 2

2011

Abstract: The Rho GTPase-activating protein Rgd1p positively regulates the GTPase activity of Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively, in the budding yeast Saccharomyces cerevisiae. Two-hybrid screening identified Tos2p as a ...

Abstract	The Rho GTPase-activating protein Rgd1p positively regulates the GTPase activity of Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively, in the budding yeast Saccharomyces cerevisiae. Two-hybrid screening identified Tos2p as a candidate Rgd1p-binding protein. Further analyses confirmed that Tos2p binds to the RhoGAP Rgd1p through its C-terminal region. Both Tos2p and Rgd1p are localized to polarized growth sites during the cell cycle and associated with detergent-resistant membranes. We observed that TOS2 overexpression suppressed rgd1Δ sensitivity to a low pH. In the tos2Δ strain, the amount of GTP-bound Rho3p was increased, suggesting an influence of Tos2p on Rgd1p activity in vivo. We also showed a functional interaction between the TOS2 and the RHO3 genes: TOS2 overexpression partially suppressed the growth defect of rho3-V51 cells at a restrictive temperature. We propose that Tos2p, a protein involved in polarized growth and most probably associated with the plasma membrane, modulates the action of Rgd1p and Rho3p in S. cerevisiae.
Language	English
Dates of publication	2011-03
Size	p. 179-191.
Publishing place	Blackwell Publishing Ltd
Document type	Article
ZDB-ID	2036775-2
ISSN	1567-1364 ; 1567-1356
ISSN (online)	1567-1364
ISSN	1567-1356
DOI	10.1111/j.1567-1364.2010.00704.x
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Zs.A 5454: Show issues

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Article: Phosphoinositides Affect both the Cellular Distribution and Activity of the F-BAR-containing RhoGAP Rgd1p in Yeast

Prouzet-Mauléon, Valérie / Lefebvre, Fabien / Thoraval, Didier / Crouzet, Marc / Doignon, François

Journal of biological chemistry. 2008 Nov. 28, v. 283, no. 48

2008

Abstract: Cell polarity is a key element of development in most eukaryotes. The Rho GTPase-activating protein Rgd1p positively regulates the GTPase activity of Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively, in the budding yeast ... ...

Abstract	Cell polarity is a key element of development in most eukaryotes. The Rho GTPase-activating protein Rgd1p positively regulates the GTPase activity of Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively, in the budding yeast Saccharomyces cerevisiae. Rgd1p contains an F-BAR domain at its N-terminal end in addition to its RhoGAP domain at its C-terminal end. We demonstrate here that phospholipids discriminate between the GTPase activities of Rho3p and Rho4p through Rgd1p and specifically stimulate the RhoGAP activity on Rho4p. The central region of the protein contiguous to the F-BAR domain is required for this stimulation. The F-BAR region binds to phosphoinositides in vitro and also plays a key role in the localization of Rgd1p to the bud tip and neck during the cell cycle. Studies of heat-sensitive mutants lacking phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-biphosphate suggested that Rgd1p initially binds to Golgi membranes via phosphatidylinositol 4-phosphate and is then transported to the plasma membrane, where it binds phosphatidylinositol 4,5-biphosphate. We demonstrate here the dual effects of phosphoinositides on a RhoGTPase-activating protein. Phosphoinositides both regulate the recruitment and trafficking of Rgd1p to membranes via the F-BAR domain and specifically stimulate GTPase-activating protein activity, consistent with functional interplay between lipids, RhoGAP, and its related GTPases in yeast growth.
Language	English
Dates of publication	2008-1128
Size	p. 33249-33257.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article: The Saccharomyces cerevisiae RhoGAP Rgd1 is phosphorylated by the Aurora B like kinase Ipl1

Vieillemard, Aurélie / Prouzet-Mauléon, Valérie / Hugues, Michel / Lefebvre, Fabien / Mitteau, Romain / Claverol, Stéphane / Bonneu, Marc / Crouzet, Marc / Doignon, François / Thoraval, Didier

Biochemical and biophysical research communications. 2013 Mar. 29, v. 433, no. 1

2013

Abstract: Polarized growth of the yeast Saccharomyces cerevisiae depends on different biological processes and requires several signaling pathways. Signaling is mediated through a set of proteins, which include Rho3p and Rho4p GTPases. Although these two proteins ... ...

Abstract	Polarized growth of the yeast Saccharomyces cerevisiae depends on different biological processes and requires several signaling pathways. Signaling is mediated through a set of proteins, which include Rho3p and Rho4p GTPases. Although these two proteins are involved in the control of distinct aspects of polarized growth in yeast, they have a common regulator: the Rgd1 RhoGAP protein. Here we demonstrate that Rgd1p is phosphorylated by the Aurora B like kinase Ipl1 and we observe that loss of Ipl1 function leads to a new Rgd1p distribution in a small part of the cell population.
Keywords	Saccharomyces cerevisiae ; guanosinetriphosphatase ; proteins ; signal transduction ; yeasts
Language	English
Dates of publication	2013-0329
Size	p. 1-5.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2013.02.081
Database	NAL-Catalogue (AGRICOLA)

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