Phosphatidic acid binding proteins display differential binding as a function of membrane curvature stress and chemical properties
Open accessAbstract
Phosphatidic acid (PA) is a crucial membrane phospholipid involved in de novo lipid synthesis and numerous intracellular signaling cascades. The signaling function of PA is mediated by peripheral membrane proteins that specifically recognize PA. While numerous PA-binding proteins are known, much less is known about what drives specificity of PA-protein binding. Previously, we have described the ionization properties of PA, summarized in the electrostatic-hydrogen bond switch, as one aspect that drives the specific binding of PA by PA-binding proteins. Here we focus on membrane curvature stress induced by phosphatidylethanolamine and show that many PA-binding proteins display enhanced binding as a function of negative curvature stress. This result is corroborated by the observation that positive curvature stress, induced by lyso phosphatidylcholine, abolishes PA binding of target proteins. We show, for the first time, that a novel plant PA-binding protein, Arabidopsis Epsin-like Clathrin Adaptor 1 (ECA1) displays curvature-dependence in its binding to PA. Other established PA targets examined in this study include, the plant proteins TGD2, and PDK1, the yeast proteins Opi1 and Spo20, and, the mammalian protein Raf-1 kinase and the C2 domain of the mammalian phosphatidylserine binding protein Lact as control. Based on our observations, we propose that liposome binding assays are the preferred method to investigate lipid binding compared to the popular lipid overlay assays where membrane environment is lost. The use of complex lipid mixtures is important to elucidate further aspects of PA binding proteins.
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PA can recruit and/or activate PIP5K and can locally influence membrane topology.
“PA can recruit and/or activate specific proteins such as PIP5K [55,56] and, with its cone-shaped geometry, PA can locally influence membrane topology and thus impact in membrane trafficking events [59].”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [59]
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- Authors
- Putta, P., Rankenberg, J., Korver, R. A., van Wijk, R., Munnik, T., Testerink, C., & Kooijman, E. E.
- Affiliations
- Kent State University (US)
- University of Amsterdam (NL)
- Corresponding author
- Kooijman, Edgar E.
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2016-11
- Volume
- 1858
- Issue
- 11
- Pages
- 2709-2716
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W2503071993
- Cited by
- 95
- References
- 63
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 8 · 2023: 8 · 2022: 11 · 2021: 9 · 2020: 11 · 2019: 15 · 2018: 10 · 2017: 7 · 2016: 2
- FWCI
- 5.89
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- Socio-Environmental Systems Modeling (acceptedVersion)
- UvA-DARE (University of Amsterdam) (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- National Science Foundation (CHE-1412920, 1058719)
- Netherlands Organization for Scientific Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- phosphatidic acid, protein-lipid binding, phosphatidylethanolamine, lysophosphatidylcholine, Arabidopsis thaliana, PDK1, Opi1, Raf-1, C2 domain, peripheral membrane proteins, lipid signaling
- MeSH terms
- Biological Assay, Carrier Proteins, Cell Membrane, Humans, Liposomes, Lysophosphatidylcholines, Phosphatidic Acids, Phosphatidylethanolamines, Protein Binding, Recombinant Fusion Proteins, Repressor Proteins, Saccharomyces cerevisiae, Arabidopsis, Proto-Oncogene Proteins c-raf, Phosphate-Binding Proteins, Arabidopsis Proteins, Saccharomyces cerevisiae Proteins, Adaptor Proteins, Vesicular Transport, Qb-SNARE Proteins, Qc-SNARE Proteins, 3-Phosphoinositide-Dependent Protein Kinases
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