Lipid−protein interactions for ECA1 an N-ANTH domain protein involved in stress signaling in plants

Putta, Priya; Creque, Emily; Piontkivska, Helen; Kooijman, Edgar E.

doi:10.1016/j.chemphyslip.2020.104919

Cited by 14 publications

(12 citation statements)

References 71 publications

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“…This suggests that the binding of At ECA1 requires some degree of hydrophobic interaction with the membrane. PA-binding proteins may take advantage of the presence of bulky hydrophobic residues such as tryptophan to insert themselves into the membrane interface, having a negative spontaneous curvature [ 71 ].…”

Section: Effect Of Pa On Membrane Statusmentioning

confidence: 99%

“…The Lys-rich motif of this protein is responsible for the interaction with the PA phosphomonoester moiety, while a region of nonpolar amino acids, seen in a helical wheel projection of the lysine-rich motif of CDeT11-24, may be involved in hydrophobic interactions with the acyl chain of PA [ 78 ]. His42 and His51 are thought to contribute to the pH sensitivity of the binding of PA to the Epsin-like Clathrin Adaptor 1 [ 71 ]. Non-basic amino acids could play a supporting role in PA binding and cause a change in the PA binding affinity of a protein—this could be an explanation for the differences in PA binding to the NADPH oxidases At RbohD and At RbohF [ 30 ].…”

Section: Binding Of Phosphatidic Acid To Target Proteinsmentioning

confidence: 99%

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Phosphatidic Acid in Plant Hormonal Signaling: From Target Proteins to Membrane Conformations

Kolesnikov

Kretynin

Bukhonska

et al. 2022

IJMS

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Cells sense a variety of extracellular signals balancing their metabolism and physiology according to changing growth conditions. Plasma membranes are the outermost informational barriers that render cells sensitive to regulatory inputs. Membranes are composed of different types of lipids that play not only structural but also informational roles. Hormones and other regulators are sensed by specific receptors leading to the activation of lipid metabolizing enzymes. These enzymes generate lipid second messengers. Among them, phosphatidic acid (PA) is a well-known intracellular messenger that regulates various cellular processes. This lipid affects the functional properties of cell membranes and binds to specific target proteins leading to either genomic (affecting transcriptome) or non-genomic responses. The subsequent biochemical, cellular and physiological reactions regulate plant growth, development and stress tolerance. In the present review, we focus on primary (genome-independent) signaling events triggered by rapid PA accumulation in plant cells and describe the functional role of PA in mediating response to hormones and hormone-like regulators. The contributions of individual lipid signaling enzymes to the formation of PA by specific stimuli are also discussed. We provide an overview of the current state of knowledge and future perspectives needed to decipher the mode of action of PA in the regulation of cell functions.

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Section: Effect Of Pa On Membrane Statusmentioning

confidence: 99%

Section: Binding Of Phosphatidic Acid To Target Proteinsmentioning

confidence: 99%

Phosphatidic Acid in Plant Hormonal Signaling: From Target Proteins to Membrane Conformations

Kolesnikov

Kretynin

Bukhonska

et al. 2022

IJMS

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“…HMS can cause the reorganization of plant endomembranes, wherein the redistribution of lipid-membrane protein binding is closely related to the regulation of metal homeostasis to a large extent [139]. Because of the position of membrane proteins in lipid bilayers, the structures and functions of the membrane proteins may be related to their positions in the lipids [140].…”

Section: Membrane Proteins and Lipid Remodelingmentioning

confidence: 99%

The Mechanism of Metal Homeostasis in Plants: A New View on the Synergistic Regulation Pathway of Membrane Proteins, Lipids and Metal Ions

Saleem

et al. 2021

Membranes

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Heavy metal stress (HMS) is one of the most destructive abiotic stresses which seriously affects the growth and development of plants. Recent studies have shown significant progress in understanding the molecular mechanisms underlying plant tolerance to HMS. In general, three core signals are involved in plants’ responses to HMS; these are mitogen-activated protein kinase (MAPK), calcium, and hormonal (abscisic acid) signals. In addition to these signal components, other regulatory factors, such as microRNAs and membrane proteins, also play an important role in regulating HMS responses in plants. Membrane proteins interact with the highly complex and heterogeneous lipids in the plant cell environment. The function of membrane proteins is affected by the interactions between lipids and lipid-membrane proteins. Our review findings also indicate the possibility of membrane protein-lipid-metal ion interactions in regulating metal homeostasis in plant cells. In this review, we investigated the role of membrane proteins with specific substrate recognition in regulating cell metal homeostasis. The understanding of the possible interaction networks and upstream and downstream pathways is developed. In addition, possible interactions between membrane proteins, metal ions, and lipids are discussed to provide new ideas for studying metal homeostasis in plant cells.

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“…The signaling function of DGPP may involve either specific interactions with proteins, where protein function is modulated (such as activation and inactivation), or through changes in membrane physical properties such as membrane curvature, bending rigidity, and charge. Additionally, the charge on the pyrophosphate headgroup of DGPP is likely to influence protein–lipid interactions [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

The Electrostatic Basis of Diacylglycerol Pyrophosphate—Protein Interaction

Graber

Kwarteng

Lange

et al. 2022

Cells

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Diacylglycerol pyrophosphate (DGPP) is an anionic phospholipid formed in plants, yeast, and parasites under multiple stress stimuli. It is synthesized by the phosphorylation action of phosphatidic acid (PA) kinase on phosphatidic acid, a signaling lipid with multifunctional properties. PA functions in the membrane through the interaction of its negatively charged phosphomonoester headgroup with positively charged proteins and ions. DGPP, like PA, can interact electrostatically via the electrostatic-hydrogen bond switch mechanism but differs from PA in its overall charge and shape. The formation of DGPP from PA alters the physicochemical properties as well as the structural dynamics of the membrane. This potentially impacts the molecular and ionic binding of cationic proteins and ions with the DGPP enriched membrane. However, the results of these important interactions in the stress response and in DGPP’s overall intracellular function is unknown. Here, using 31P MAS NMR, we analyze the effect of the interaction of low DGPP concentrations in model membranes with the peptides KALP23 and WALP23, which are flanked by positively charged Lysine and neutral Tryptophan residues, respectively. Our results show a significant effect of KALP23 on the charge of DGPP as compared to WALP23. There was, however, no significant effect on the charge of the phosphomonoester of DGPP due to the interaction with positively charged lipids, dioleoyl trimethylammonium propane (DOTAP) and dioleoyl ethyl-phosphatidylcholine (EtPC). Divalent calcium and magnesium cations induce deprotonation of the DGPP headgroup but showed no noticeable differences on DGPP’s charge. Our results lead to a novel model for DGPP—protein interaction.

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Lipid−protein interactions for ECA1 an N-ANTH domain protein involved in stress signaling in plants

Cited by 14 publications

References 71 publications

Phosphatidic Acid in Plant Hormonal Signaling: From Target Proteins to Membrane Conformations

Phosphatidic Acid in Plant Hormonal Signaling: From Target Proteins to Membrane Conformations

The Mechanism of Metal Homeostasis in Plants: A New View on the Synergistic Regulation Pathway of Membrane Proteins, Lipids and Metal Ions

The Electrostatic Basis of Diacylglycerol Pyrophosphate—Protein Interaction

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