A lipid transfer protein binds to a receptor involved in the control of plant defence responses

Buhot, Nathalie; Douliez, Jean‐Paul; Jacquemard, Alain; Marion, Didier; Tran, Vinh; Maume, B.F.; Milat, Marie‐Louise; Ponchet, Michel; Mikeš, Vladimír; Kader, Jean‐Claude; Blein, Jean‐Pierre

doi:10.1016/s0014-5793(01)03116-7

Cited by 152 publications

(107 citation statements)

References 32 publications

(47 reference statements)

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“…The use of LTP, a cryptogein antagonist that binds to the same high-affinity site at the plasma membrane, but triggers neither signaling events (Buhot et al, 2001) nor endocytosis (this study), emphasizes the role of signaling by cryptogein as the release mechanism for endocytosis. Interestingly, the transient wave of CCPs observed in the first 10 min after cryptogein addition exhibits the same kinetics as the typical transient production of ROS (Simon-Plas et al, 1997).…”

Section: Ros Production Is Correlated With Endocytosismentioning

confidence: 83%

“…In tobacco cells, both cryptogein and an LTP1 from wheat (Triticum aestivum) bind to an identical high-affinity specific site located on the plasma membrane (Buhot et al, 2001). In addition, in vivo competition experiments have indicated that the binding sites for both proteins are their true biological receptor because addition of increasing concentrations of LTP1 reduced signaling events induced by cryptogein (Buhot et al, 2001). Nevertheless, LTP alone did not trigger any of the classical responses induced by cryptogein in tobacco cells, such as extracellular alkalinization or oxidative burst.…”

Section: Endocytosis Requires Not Only Binding To the Receptor But Amentioning

confidence: 99%

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The Plant Defense Elicitor Cryptogein Stimulates Clathrin-Mediated Endocytosis Correlated with Reactive Oxygen Species Production in Bright Yellow-2 Tobacco Cells

et al. 2008

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The plant defense elicitor cryptogein triggers well-known biochemical events of early signal transduction at the plasma membrane of tobacco (Nicotiana tabacum) cells, but microscopic observations of cell responses related to these early events were lacking. We determined that internalization of the lipophilic dye FM4-64, which is a marker of endocytosis, is stimulated a few minutes after addition of cryptogein to tobacco Bright Yellow-2 (BY-2) cells. This stimulation is specific to the signal transduction pathway elicited by cryptogein because a lipid transfer protein, which binds to the same receptor as cryptogein but without triggering signaling, does not increase endocytosis. To define the nature of the stimulated endocytosis, we quantified clathrin-coated pits (CCPs) forming on the plasma membrane of BY-2 cells. A transitory stimulation of this morphological event by cryptogein occurs within the first 15 min. In the presence of cryptogein, increases in both FM4-64 internalization and clathrin-mediated endocytosis are specifically blocked upon treatment with 5 mM tyrphostin A23, a receptor-mediated endocytosis inhibitor. The kinetics of the transient increase in CCPs at the plasma membrane coincides with that of transitory reactive oxygen species (ROS) production occurring within the first 15 min after elicitation. Moreover, in BY-2 cells expressing NtrbohD antisense cDNA, which are unable to produce ROS when treated with cryptogein, the CCP stimulation is inhibited. These results indicate that the very early endocytic process induced by cryptogein in tobacco is due, at least partly, to clathrin-mediated endocytosis and is dependent on ROS production by the NADPH oxidase NtrbohD.

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Section: Ros Production Is Correlated With Endocytosismentioning

confidence: 83%

Section: Endocytosis Requires Not Only Binding To the Receptor But Amentioning

confidence: 99%

The Plant Defense Elicitor Cryptogein Stimulates Clathrin-Mediated Endocytosis Correlated with Reactive Oxygen Species Production in Bright Yellow-2 Tobacco Cells

et al. 2008

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“…Thirdly, a kinetic analysis of the elicitin binding curves, using the allosteric model of Monod [58], confirms that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits [59]. Taking these results into account, we proposed that the elicitin receptor could be a ligand-dependent calcium channel constituted of a quadrimeric complex as shown in Figure 3, which summarizes the initial molecular events involving activation of elicitin by sterol loading that drive the elicitor function [56,59].Finally, all the elicitins tested are able to bind to the same sites (with a similar affinity), suggesting that they are recognized by the same receptors, although they induce differential cell and plant responses [40]. These apparently contradictory observations remained to be explained.…”

mentioning

confidence: 64%

“…Finally, the effects of LTP1 on tobacco cells were analyzed. The addition of increasing concentrations of LTP1 reduced the production of active oxygen species, induced by a fixed cryptogein concentration [59]. This result indicates that the binding sites of LTP1 and cryptogein are their true biological receptors.…”

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confidence: 74%

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Involvement of lipid-protein complexes in plant-microorganism interactions

Blein¹

2002

OCL

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Summary : Increasing concerns about the environmental impact of modern agricultural have prompted research for alternate practices to pesticide treatments, notably using plant defense mechanisms. Thus, isolation and characterization of plant defense elicitors have been the main step of studies in many groups. Moreover, in the global concept of interactions between organisms and their environment, a major concern is to discriminate recognition between exogenous and endogenous signals, notably during pathogenic or allergenic interactions involving small proteins, such as elicitins or lipid transfer proteins (LTPs). Elicitins and lipid transfer proteins (LTP) are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defense mechanisms, the biological function of LTPs is still an enigma. They are ubiquitous plant proteins able to load and transfer hydrophobic molecules such as fatty acids or phospholipids. Among them, LTPs1 (type 1 lipid transfer proteins) constitute a multigenic family of secreted plant lipid binding proteins that are constitutively expressed in specific tissues and/or induced in response to biotic and abiotic stress (for reviews [1][2][3][4]). Their biological function is still unknown, even if some data provide arguments for a role of these proteins in the assembly of extracellular hydrophobic polymers (i.e., cutin and suberin) [2,4] and/or in plant defense against fungal pathogens [1,3]. Beside their involvement in plant defense, LTPs1 are also known to be pan-allergens of plant-derived foods [5]. Finally, the discovery of the sterol carrier-properties of elicitins has opened new perspectives dealing with the relationship between this function and the elicitor activity of these small cystein-rich proteins. Nevertheless, this elicitor activity is restrained to few plant species, and thus does not appear in accordance with a universal lipid transfer function. These considerations required a reassessment of the precise role of elicitins for both fungi and plants [6].Résumé : La stimulation des mécanismes naturels de défense des plantes représente une stratégie alternative à l'utilisation de la lutte chimique en phytoprotection. Dans ce contexte, les élicitines, qui sont de petites protéines sécrétées par des Phytophthora et des Pythium, induisent une réaction de type hypersensible chez des plantes comme le tabac. Ces plantes deviennent résistantes à l'agression de leurs agents pathogènes. La récente découverte que les élicitines sont des protéines de transfert de stérols a apporté une vue nouvelle sur l'activité moléculaire des élicitines. Élicitines et protéines de transfert de lipides (LTP) sont capables de charger et de transporter des molécules lipidiques et partagent des caractères communs tant au plan structural que fonctionnel mais, tandis que les élicitines sont connues pour leur activité élicitrice de réaction de défense chez les plantes, l'activité biologique des LTP reste inconnue. Cependant, ...

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Plant Lipid Transfer Proteins: Relationships Between Allergenicity and Structural, Biological and Technological Properties

Marion¹,

Douliez²,

Gautier³

et al. 2003

Plant Food Allergens

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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

Cited by 152 publications

References 32 publications

The Plant Defense Elicitor Cryptogein Stimulates Clathrin-Mediated Endocytosis Correlated with Reactive Oxygen Species Production in Bright Yellow-2 Tobacco Cells

The Plant Defense Elicitor Cryptogein Stimulates Clathrin-Mediated Endocytosis Correlated with Reactive Oxygen Species Production in Bright Yellow-2 Tobacco Cells

Involvement of lipid-protein complexes in plant-microorganism interactions

Plant Lipid Transfer Proteins: Relationships Between Allergenicity and Structural, Biological and Technological Properties

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