Protein–Phospholipid Interaction Motifs: A Focus on Phosphatidic Acid

Tanguy, Emeline; Kassas, Nawal; Vitale, Nicolas

doi:10.3390/biom8020020

Cited by 61 publications

(74 citation statements)

References 31 publications

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“…In some of these assays, lipids were immobilized on nitrocellulose filter , coupled to the beads , or organized into liposomes . These assays are well discussed in Refs . The liposome‐based assay is the most used one because of the advantage that liposomes form a membrane bilayer mimicking the natural arrangement of lipids .…”

Section: Chemical Properties Of Pamentioning

confidence: 99%

“…These assays are well discussed in Refs . The liposome‐based assay is the most used one because of the advantage that liposomes form a membrane bilayer mimicking the natural arrangement of lipids .…”

Section: Chemical Properties Of Pamentioning

confidence: 99%

“…In the studies of PA-protein interactions, various assays were used. In some of these assays, lipids were These assays are well discussed in Refs [3,82,83]. The liposome-based assay is the most used one because of the advantage that liposomes form a membrane bilayer mimicking the natural arrangement of lipids [3,82].…”

Section: Pa-protein Interactionsmentioning

confidence: 99%

“…In lysophosphatidic acid (LPA), or 1‐acyl‐ sn ‐glycero‐3‐phosphate, only one fatty acid is bonded to carbon‐1. PA is a minor membrane phospholipid, it usually constitutes 1‐4% of membrane lipids . However, this substance is present in virtually all cellular membranes ( and references therein).…”

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confidence: 99%

“…In lysophosphatidic acid (LPA), or 1-acyl-sn-glycero-3phosphate, only one fatty acid is bonded to carbon-1. PA is a minor membrane phospholipid, it usually Abbreviations AGPAT4, acylglycerophosphate acyltransferase type 4; C2 domain, second conserved domain of protein kinase C; Cer-1-P, ceramide-1-phosphate; CtBP1-S/BARS, C-terminal-binding protein 1-short form/brefeldin A ADP-ribosylation substrate; DAG, diacylglycerol; DAGPP, diacylglycerolpyrophosphate; DGKs, diacylglycerol kinases; DHAP, dihydroxyacetone phosphate; DOPC, dioleoyl phosphatidylcholine; Drp1, dynamin-related protein 1; EEA1, Early Endosome Antigen 1; F-BAR domain, FCH-Bin/amphiphysin/RVS domain; FYVE domain, Fab 1-YOTB-Vac 1-EEA1 domain; G3P, glycerol-3-phosphate; LPA, lysophosphatidic acid; LPAAT, lysophosphatidic acid acyltransferase; LPC, lysophosphatidylcholine; MICAL-L1, molecule interacting with CasL-Like1; Munc13, mammalian uncoordinated 13; NSF, N-ethylmaleimide-sensitive factor; PA, phosphatidic acid; Pah1, phosphatidic acid phosphatase 1; PAK, p21-activated kinase; PAP, phosphatidic acid phosphatase; PA-PLA1, phosphatidic acid-selective phospholipase A1; PC, phosphatidylcholine; PE, phosphatidylethanolamine; PG, phosphatidylglycerol; PH domain, Pleckstrin Homology domain; PI, phosphatidylinositol; PIPs, phosphatidylinositol phosphates; PKCs, protein kinases C; PKDs, protein kinases D; PLA, phospholipase A; PLD, phospholipase D; PS, phosphatidylserine; PtdIns(4,5)P 2 , phosphatidylinositol-4,5-bisphosphate; PtdIns4P, phosphatidylinositol-4-phosphate; PtdIns4P5K, phosphatidylinositol-4-phosphate-5-kinase; PX domain, phox (phagocyte oxidase) homology domain; RasGRPs, Ras guanyl nucleotide-releasing proteins; SNARE, soluble N-ethylmaleimide-sensitive factor attachment protein receptor; TGN, trans-Golgi network; Unc-13, uncoordinated protein 13; Vps1p, vacuolar protein sorting-associated protein 1. constitutes 1-4% of membrane lipids [2][3][4][5][6]. However, this substance is present in virtually all cellular membranes ( [7] and references therein).…”

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Phosphatidic acid in membrane rearrangements

et al. 2019

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Phosphatidic acid (PA) is the simplest cellular glycerophospholipid characterized by unique biophysical properties: a small headgroup; negative charge; and a phosphomonoester group. Upon interaction with lysine or arginine, PA charge increases from −1 to −2 and this change stabilizes protein–lipid interactions. The biochemical properties of PA also allow interactions with lipids in several subcellular compartments. Based on this feature, PA is involved in the regulation and amplification of many cellular signalling pathways and functions, as well as in membrane rearrangements. Thereby, PA can influence membrane fusion and fission through four main mechanisms: it is a substrate for enzymes producing lipids (lysophosphatidic acid and diacylglycerol) that are involved in fission or fusion; it contributes to membrane rearrangements by generating negative membrane curvature; it interacts with proteins required for membrane fusion and fission; and it activates enzymes whose products are involved in membrane rearrangements. Here, we discuss the biophysical properties of PA in the context of the above four roles of PA in membrane fusion and fission.

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Section: Chemical Properties Of Pamentioning

confidence: 99%

Section: Chemical Properties Of Pamentioning

confidence: 99%

Section: Pa-protein Interactionsmentioning

confidence: 99%

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Phosphatidic acid in membrane rearrangements

et al. 2019

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Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria

2021

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The mechanisms controlling membrane recognition by proteins with one hydrophobic stretch at their carboxyl terminus (tail anchor, TA) are poorly defined. The Escherichia coli TAs of ElaB and YqjD, which share sequential and structural similarity with the Saccharomyces cerevisiae TA of Fis1, were shown to localize to mitochondria. We show that YqjD and ElaB are directed by their TAs to bacterial cell poles. Fis1(TA) expressed in E. coli localizes like the endogenous TAs. The yeast and bacterial TAs are inserted in the E. coli inner membrane, and they all show affiliation to phosphatidic acid (PA), found in the membrane of the bacterial cell poles and of the yeast mitochondria. Our results suggest a mechanism for TA membrane recognition conserved from bacteria to mitochondria and raise the possibility that through their interaction with PA, and TAs play a role across prokaryotes and eukaryotes in controlling cell/organelle fate.

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Rapid Formation of Non‐canonical Phospholipid Membranes by Chemoselective Amide‐Forming Ligations with Hydroxylamines**

Chen,

Brea,

Fracassi

et al. 2023

Angewandte Chemie

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There has been increasing interest in methods to generate synthetic lipid membranes as key constituents of artificial cells or to develop new tools for remodeling membranes in living cells. However, the biosynthesis of phospholipids involves elaborate enzymatic pathways that are challenging to reconstitute in vitro. An alternative approach is to use chemical reactions to non‐enzymatically generate natural or non‐canonical phospholipids de novo. Previous reports have shown that synthetic lipid membranes can be formed in situ using various ligation chemistries, but these methods lack biocompatibility and/or suffer from slow kinetics at physiological pH. Thus, it would be valuable to develop chemoselective strategies for synthesizing phospholipids from water‐soluble precursors that are compatible with synthetic or living cells Here, we demonstrate that amide‐forming ligations between lipid precursors bearing hydroxylamines and α‐ketoacids (KAs) or potassium acyltrifluoroborates (KATs) can be used to prepare non‐canonical phospholipids at physiological pH conditions. The generated amide‐linked phospholipids spontaneously self‐assemble into cell‐like micron‐sized vesicles similar to natural phospholipid membranes. We show that lipid synthesis using KAT ligation proceeds extremely rapidly, and the high selectivity and biocompatibility of the approach facilitates the in situ synthesis of phospholipids and associated membranes in living cells.

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Protein–Phospholipid Interaction Motifs: A Focus on Phosphatidic Acid

Cited by 61 publications

References 31 publications

Phosphatidic acid in membrane rearrangements

Phosphatidic acid in membrane rearrangements

Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria

Rapid Formation of Non‐canonical Phospholipid Membranes by Chemoselective Amide‐Forming Ligations with Hydroxylamines**

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