Gevaert K

References (9)

Title : A Phelipanche ramosa KAI2 protein perceives strigolactones and isothiocyanates enzymatically - de Saint Germain_2021_Plant.Commun_2_100166
Author(s) : de Saint Germain A , Jacobs A , Brun G , Pouvreau JB , Braem L , Cornu D , Clave G , Baudu E , Steinmetz V , Servajean V , Wicke S , Gevaert K , Simier P , Goormachtig S , Delavault P , Boyer FD
Ref : Plant Commun , 2 :100166 , 2021
Abstract : Phelipanche ramosa is an obligate root-parasitic weed that threatens major crops in central Europe. In order to germinate, it must perceive various structurally divergent host-exuded signals, including isothiocyanates (ITCs) and strigolactones (SLs). However, the receptors involved are still uncharacterized. Here, we identify five putative SL receptors in P. ramosa and show that PrKAI2d3 is involved in the stimulation of seed germination. We demonstrate the high plasticity of PrKAI2d3, which allows it to interact with different chemicals, including ITCs. The SL perception mechanism of PrKAI2d3 is similar to that of endogenous SLs in non-parasitic plants. We provide evidence that PrKAI2d3 enzymatic activity confers hypersensitivity to SLs. Additionally, we demonstrate that methylbutenolide-OH binds PrKAI2d3 and stimulates P. ramosa germination with bioactivity comparable to that of ITCs. This study demonstrates that P. ramosa has extended its signal perception system during evolution, a fact that should be considered for the development of specific and efficient biocontrol methods.
ESTHER : de Saint Germain_2021_Plant.Commun_2_100166
PubMedSearch : de Saint Germain_2021_Plant.Commun_2_100166
PubMedID: 34746757
Gene_locus related to this paper: phera-PrKAI2c , phera-PrKAI2d1 , phera-PrKAI2d2 , phera-PrKAI2d3 , phera-PrKAI2d4

Title : A Phelipanche ramosa KAI2 Protein Perceives enzymatically Strigolactones and Isothiocyanates - de Saint Germain_2020_Biorxiv__
Author(s) : de Saint Germain A , Jacobs A , Brun G , Pouvreau JB , Braem L , Cornu D , Clave G , Baudu E , Steinmetz V , Servajean V , Wicke S , Gevaert K , Simier P , Goormachti S , Delavault P , Boyer FD
Ref : Biorxiv , : , 2020
Abstract : Phelipanche ramosa is an obligate root-parasitic weed threatening major crops in central Europe. For its germination, it has to perceive various structurally diverging host-exuded signals, including isothiocyanates (ITCs) and strigolactones (SLs). However, the receptors involved are still uncharacterized. Here, we identified five putative SL receptors in P. ramosa, of which PrKAI2d3 is involved in seed germination stimulation. We established the high plasticity of PrKAI2d3, allowing interaction with different chemicals, including ITCs. The SL perception mechanism of PrKAI2d3 is similar to that of endogenous SLs in non-parasitic plants. We provide evidence that the PrKAI2d3 enzymatic activity confers hypersensitivity to SLs. Additionally, we demonstrated that methylbutenolide-OH binds PrKAI2d3 and stimulates P. ramosa germination with a bioactivity comparable to that of ITCs. This study highlights that P. ramosa has extended its signal perception system during evolution, a fact to be considered in the development of specific and efficient biocontrol methods.
ESTHER : de Saint Germain_2020_Biorxiv__
PubMedSearch : de Saint Germain_2020_Biorxiv__
PubMedID:

Title : Unraveling the MAX2 Protein Network in Arabidopsis thaliana: Identification of the Protein Phosphatase PAPP5 as a Novel MAX2 Interactor - Struk_2020_Mol.Cell.Proteomics__
Author(s) : Struk S , De Cuyper C , Jacobs A , Braem L , Walton A , De Keyser A , Depuydt S , Vu LD , De Smet I , Boyer FD , Eeckhout D , Persiau G , Gevaert K , De Jaeger G , Goormachtig S
Ref : Mol Cell Proteomics , : , 2020
Abstract : The F-box protein MORE AXILLARY GROWTH 2 (MAX2) is a central component in the signaling cascade of strigolactones (SLs) as well as of the smoke derived karrikins (KARs) and the so far unknown endogenous KAI2 ligand (KL). The two groups of molecules are involved in overlapping and unique developmental processes, and signal-specific outcomes are attributed to perception by the paralogous alpha/beta-hydrolases DWARF14 (D14) for SL and KARRIKIN INSENSITIVE 2/ HYPOSENSITIVE TO LIGHT (KAI2/HTL) for KAR/KL. Additionally, depending on which receptor is activated, specific members of the SUPPRESSOR OF MAX2 1 (SMAX1) - LIKE (SMXL) family control KAR/KL and SL responses. As proteins that function in the same signal transduction pathway often occur in large protein complexes, we aimed at discovering new players of the MAX2, D14 and KAI2 protein network by tandem affinity purification using Arabidopsis cell cultures. When using MAX2 as a bait, various proteins were co-purified among which general components of the Skp1-Cullin-F-box complex and members of the CONSTITUTIVE PHOTOMORPHOGENIC 9 signalosome. Here, we report the identification of a novel interactor of MAX2, a type 5 serine/threonine protein phosphatase, designated PHYTOCHROME-ASSOCIATED PROTEIN PHOSPHATASE 5 (PAPP5). Quantitative affinity purification pointed at PAPP5 as being more present in KAI2 rather than D14 protein complexes. In agreement, mutant analysis suggests that PAPP5 modulates KAR/KL-dependent seed germination in suboptimal conditions and seedling development. Additionally, a phosphopeptide enrichment experiment revealed that PAPP5 might dephosphorylate MAX2 in vivo independently of the synthetic strigolactone analog, rac-GR24. Together, by analyzing the protein complexes to which MAX2, D14 and KAI2 belong, we revealed a new MAX2 interactor, PAPP5, that might act through dephosphorylation of MAX2 to control mainly KAR/KL- related phenotypes and, hence, provide another link with the light pathway.
ESTHER : Struk_2020_Mol.Cell.Proteomics__
PubMedSearch : Struk_2020_Mol.Cell.Proteomics__
PubMedID: 33372050

Title : Impairment of Angiogenesis by Fatty Acid Synthase Inhibition Involves mTOR Malonylation - Bruning_2018_Cell.Metab_28_866
Author(s) : Bruning U , Morales-Rodriguez F , Kalucka J , Goveia J , Taverna F , Queiroz KCS , Dubois C , Cantelmo AR , Chen R , Loroch S , Timmerman E , Caixeta V , Bloch K , Conradi LC , Treps L , Staes A , Gevaert K , Tee A , Dewerchin M , Semenkovich CF , Impens F , Schilling B , Verdin E , Swinnen JV , Meier JL , Kulkarni RA , Sickmann A , Ghesquiere B , Schoonjans L , Li X , Mazzone M , Carmeliet P
Ref : Cell Metab , 28 :866 , 2018
Abstract : The role of fatty acid synthesis in endothelial cells (ECs) remains incompletely characterized. We report that fatty acid synthase knockdown (FASN(KD)) in ECs impedes vessel sprouting by reducing proliferation. Endothelial loss of FASN impaired angiogenesis insvivo, while FASN blockade reduced pathological ocular neovascularization, at >10-fold lower doses than used for anti-cancer treatment. Impaired angiogenesis was not due to energy stress, redox imbalance, or palmitate depletion. Rather, FASN(KD) elevated malonyl-CoA levels, causing malonylation (a post-translational modification) of mTOR at lysine 1218 (K1218). mTOR K-1218 malonylation impaired mTOR complex 1 (mTORC1) kinase activity, thereby reducing phosphorylation of downstream targets (p70S6K/4EBP1). Silencing acetyl-CoA carboxylase 1 (an enzyme producing malonyl-CoA) normalized malonyl-CoA levels and reactivated mTOR in FASN(KD) ECs. Mutagenesis unveiled the importance of mTOR K1218 malonylation for angiogenesis. This study unveils a novel role of FASN in metabolite signaling that contributes to explaining the anti-angiogenic effect of FASN blockade.
ESTHER : Bruning_2018_Cell.Metab_28_866
PubMedSearch : Bruning_2018_Cell.Metab_28_866
PubMedID: 30146486

Title : Strigolactones, karrikins and beyond - De Cuyper_2017_Plant.Cell.Environ_40_1691
Author(s) : De Cuyper C , Struk S , Braem L , Gevaert K , De Jaeger G , Goormachtig S
Ref : Plant Cell Environ , 40 :1691 , 2017
Abstract : The plant hormones strigolactones are synthesized from carotenoids and signal via the alpha/beta hydrolase DWARF 14 (D14) and the F-box protein MORE AXILLARY GROWTH 2 (MAX2). Karrikins, molecules produced upon fire, share MAX2 for signalling, but depend on the D14 paralog KARRIKIN INSENSITIVE 2 (KAI2) for perception with strong evidence that the MAX2-KAI2 protein complex might also recognize so far unknown plant-made karrikin-like molecules. Thus, the phenotypes of the max2 mutants are the complex consequence of a loss of both D14-dependent and KAI2-dependent signalling, hence, the reason why some biological roles, attributed to strigolactones based on max2 phenotypes, could never be observed in d14 or in the strigolactone-deficient max3 and max4 mutants. Moreover, the broadly used synthetic strigolactone analog rac-GR24 has been shown to mimic strigolactone as well as karrikin(-like) signals, providing an extra level of complexity in the distinction of the unique and common roles of both molecules in plant biology. Here, a critical overview is provided of the diverse biological processes regulated by strigolactones and/or karrikins. These two growth regulators are considered beyond their boundaries, and the importance of the yet unknown karrikin-like molecules is discussed as well.
ESTHER : De Cuyper_2017_Plant.Cell.Environ_40_1691
PubMedSearch : De Cuyper_2017_Plant.Cell.Environ_40_1691
PubMedID: 28558130

Title : The Response of the Root Proteome to the Synthetic Strigolactone GR24 in Arabidopsis - Walton_2016_Mol.Cell.Proteomics_15_2744
Author(s) : Walton A , Stes E , Goeminne G , Braem L , Vuylsteke M , Matthys C , De Cuyper C , Staes A , Vandenbussche J , Boyer FD , Vanholme R , Fromentin J , Boerjan W , Gevaert K , Goormachtig S
Ref : Mol Cell Proteomics , 15 :2744 , 2016
Abstract : Strigolactones are plant metabolites that act as phytohormones and rhizosphere signals. Whereas most research on unraveling the action mechanisms of strigolactones is focused on plant shoots, we investigated proteome adaptation during strigolactone signaling in the roots of Arabidopsis thaliana. Through large-scale, time-resolved, and quantitative proteomics, the impact of the strigolactone analog rac-GR24 was elucidated on the root proteome of the wild type and the signaling mutant more axillary growth 2 (max2). Our study revealed a clear MAX2-dependent rac-GR24 response: an increase in abundance of enzymes involved in flavonol biosynthesis, which was reduced in the max2-1 mutant. Mass spectrometry-driven metabolite profiling and thin-layer chromatography experiments demonstrated that these changes in protein expression lead to the accumulation of specific flavonols. Moreover, quantitative RT-PCR revealed that the flavonol-related protein expression profile was caused by rac-GR24-induced changes in transcript levels of the corresponding genes. This induction of flavonol production was shown to be activated by the two pure enantiomers that together make up rac-GR24. Finally, our data provide much needed clues concerning the multiple roles played by MAX2 in the roots and a comprehensive view of the rac-GR24-induced response in the root proteome.
ESTHER : Walton_2016_Mol.Cell.Proteomics_15_2744
PubMedSearch : Walton_2016_Mol.Cell.Proteomics_15_2744
PubMedID: 27317401

Title : The Whats, the Wheres and the Hows of strigolactone action in the roots - Matthys_2016_Planta_243_1327
Author(s) : Matthys C , Walton A , Struk S , Stes E , Boyer FD , Gevaert K , Goormachtig S
Ref : Planta , 243 :1327 , 2016
Abstract : Strigolactones control various aspects of plant development, including root architecture. Here, we review how strigolactones act in the root and survey the strigolactone specificity of signaling components that affect root development. Strigolactones are a group of secondary metabolites produced in plants that have been assigned multiple roles, of which the most recent is hormonal activity. Over the last decade, these compounds have been shown to regulate various aspects of plant development, such as shoot branching and leaf senescence, but a growing body of literature suggests that these hormones play an equally important role in the root. In this review, we present all known root phenotypes linked to strigolactones. We examine the expression and presence of the main players in biosynthesis and signaling of these hormones and bring together the available information that allows us to explain how strigolactones act to modulate the root system architecture.
ESTHER : Matthys_2016_Planta_243_1327
PubMedSearch : Matthys_2016_Planta_243_1327
PubMedID: 26895337

Title : Proteome-wide characterization of N-glycosylation events by diagonal chromatography - Ghesquiere_2006_J.Proteome.Res_5_2438
Author(s) : Ghesquiere B , Van Damme J , Martens L , Vandekerckhove J , Gevaert K
Ref : J Proteome Res , 5 :2438 , 2006
Abstract : A procedure to map N-glycosylation sites is presented here. It can be applied to purified proteins as well as to highly complex mixtures. The method exploits deglycosylation by PNGase F in a diagonal, reverse-phase chromatographic setup. When applied to 10 microL of mouse serum, affinity-depleted for its three most abundant components, 117 known or predicted sites were mapped in addition to 10 novel sites. Several sites were detected on soluble membrane or receptor components. Our method furthermore senses the nature of glycan structures and can detect differential glycosylation on a given site. These properties--high sensitivity and dependence on glycan imprinting--can be exploited for glycan-biomarker analysis.
ESTHER : Ghesquiere_2006_J.Proteome.Res_5_2438
PubMedSearch : Ghesquiere_2006_J.Proteome.Res_5_2438
PubMedID: 16944957
Gene_locus related to this paper: mouse-Ces1c

Title : Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides - Gevaert_2003_Nat.Biotechnol_21_566
Author(s) : Gevaert K , Goethals M , Martens L , Van Damme J , Staes A , Thomas GR , Vandekerckhove J
Ref : Nat Biotechnol , 21 :566 , 2003
Abstract : Current non-gel techniques for analyzing proteomes rely heavily on mass spectrometric analysis of enzymatically digested protein mixtures. Prior to analysis, a highly complex peptide mixture is either separated on a multidimensional chromatographic system or it is first reduced in complexity by isolating sets of representative peptides. Recently, we developed a peptide isolation procedure based on diagonal electrophoresis and diagonal chromatography. We call it combined fractional diagonal chromatography (COFRADIC). In previous experiments, we used COFRADIC to identify more than 800 Escherichia coli proteins by tandem mass spectrometric (MS/MS) analysis of isolated methionine-containing peptides. Here, we describe a diagonal method to isolate N-terminal peptides. This reduces the complexity of the peptide sample, because each protein has one N terminus and is thus represented by only one peptide. In this new procedure, free amino groups in proteins are first blocked by acetylation and then digested with trypsin. After reverse-phase (RP) chromatographic fractionation of the generated peptide mixture, internal peptides are blocked using 2,4,6-trinitrobenzenesulfonic acid (TNBS); they display a strong hydrophobic shift and therefore segregate from the unaltered N-terminal peptides during a second identical separation step. N-terminal peptides can thereby be specifically collected for further liquid chromatography (LC)-MS/MS analysis. Omitting the acetylation step results in the isolation of non-lysine-containing N-terminal peptides from in vivo blocked proteins.
ESTHER : Gevaert_2003_Nat.Biotechnol_21_566
PubMedSearch : Gevaert_2003_Nat.Biotechnol_21_566
PubMedID: 12665801
Gene_locus related to this paper: human-ABHD16A