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Membranes
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Membrane Domains Organization and Interactions
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Membrane Domains Organization and Interactions

A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membrane Composition and Structures".

Deadline for manuscript submissions: closed (10 May 2022) | Viewed by 20503

Special Issue Editors

Dr. Agnieszka Polit

E-Mail Website
Guest Editor
Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University in Kraków, ul. Gronostajowa 7, 30-387 Kraków, Poland
Interests: cellular membrane structures; protein-lipid interactions; molecular recognition; lipid domains; membrane protein targeting; signalling pathways; G protein-coupled receptors, biological spectroscopy
Special Issues, Collections and Topics in MDPI journals
Dr. Paweł Mystek

E-Mail Website
Guest Editor
Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University in Kraków, ul. Gronostajowa 7, 30-387 Kraków, Poland
Interests: lipid-anchored proteins; membrane protein lateral diffusion; cellular membrane structures; protein-lipid interactions; signaling in cells; fluorescence microscopy
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Our knowledge of biological membranes has substantially changed over the past several years, from the fluid mosaic idea to the current concept of lipids and proteins separating into microdomains that differ in their protein and lipid compositions. The role of lipids and membrane proteins is not limited to constituting the cell barrier. They are also involved in a wide range of processes including intracellular and extracellular transport, communication, cell migration, cell shape formation, and participation in the mechanisms of signal transduction that regulate cell function and homeostasis. Investigation of the world of membrane domains and the function of specific protein–lipid complexes has become possible thanks to the novel advanced tools used to study functions of diverse lipid classes in membranes with structural analysis and simulations at the atomic resolution. This Special Issue will highlight the importance of the membrane domains in protein–lipid interactions and the implications of this role on our understanding of the overall organization and functioning of cell membranes and their relation to myriad cellular outcomes. We seek submissions of experimental and computational approaches focused on protein–lipid interactions on molecular and membrane levels. Reviews on promising methods or techniques for studying membrane organization and molecular interactions are also highly welcome.

Dr. Agnieszka Polit
Dr. Paweł Mystek
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Membranes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Biological membranes
  • Lipid domains
  • Membrane organization
  • Model membranes
  • Lipid–protein interactions
  • Lipid rafts
  • Molecular recognition
  • Membrane regulation of signal transduction
  • Membrane protein clustering
  • Protein-enriched domains
  • Membrane protein diffusion
  • Membrane domain targeting
  • Plasma membrane compartmentalization
  • Molecular dynamics simulation
  • Lipid binding motifs

Published Papers (6 papers)

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Research

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31 pages, 5256 KiB  
Article
Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin
by Divya Teja Dondapati, Pradeep Reddy Cingaram, Ferhan Ayaydin, Antal Nyeste, Andor Kanyó, Ervin Welker and Elfrieda Fodor
Membranes 2021, 11(12), 978; https://doi.org/10.3390/membranes11120978 - 13 Dec 2021
Cited by 1 | Viewed by 3277
Abstract
The cellular prion protein (PrPC) is renowned for its infectious conformational isoform PrPSc, capable of templating subsequent conversions of healthy PrPCs and thus triggering the group of incurable diseases known as transmissible spongiform encephalopathies. Besides this mechanism [...] Read more.
The cellular prion protein (PrPC) is renowned for its infectious conformational isoform PrPSc, capable of templating subsequent conversions of healthy PrPCs and thus triggering the group of incurable diseases known as transmissible spongiform encephalopathies. Besides this mechanism not being fully uncovered, the protein’s physiological role is also elusive. PrPC and its newest, less understood paralog Shadoo are glycosylphosphatidylinositol-anchored proteins highly expressed in the central nervous system. While they share some attributes and neuroprotective actions, opposing roles have also been reported for the two; however, the amount of data about their exact functions is lacking. Protein–protein interactions and membrane microdomain localizations are key determinants of protein function. Accurate identification of these functions for a membrane protein, however, can become biased due to interactions occurring during sample processing. To avoid such artifacts, we apply a non-detergent-based membrane-fractionation approach to study the prion protein and Shadoo. We show that the two proteins occupy similarly raft and non-raft membrane fractions when expressed in N2a cells and that both proteins pull down the chaperone calnexin in both rafts and non-rafts. These indicate their possible binding to calnexin in both types of membrane domains, which might be a necessary requisite to aid the inherently unstable native conformation during their lifetime. Full article
(This article belongs to the Special Issue Membrane Domains Organization and Interactions)
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17 pages, 2584 KiB  
Article
O-GlcNAcylation Inhibits Endocytosis of Amyloid Precursor Protein by Decreasing Its Localization in Lipid Raft Microdomains
by Oh-Hoon Kwon, Yoon Young Cho, Jung Hee Lee and Sungkwon Chung
Membranes 2021, 11(12), 909; https://doi.org/10.3390/membranes11120909 - 23 Nov 2021
Cited by 3 | Viewed by 1917
Abstract
Like protein phosphorylation, O-GlcNAcylation is a common post-translational protein modification. We already reported that O-GlcNAcylation of amyloid precursor protein (APP) in response to insulin signaling reduces neurotoxic amyloid-β (Aβ) production via inhibition of APP endocytosis. Internalized APP is delivered to endosomes and lysosomes [...] Read more.
Like protein phosphorylation, O-GlcNAcylation is a common post-translational protein modification. We already reported that O-GlcNAcylation of amyloid precursor protein (APP) in response to insulin signaling reduces neurotoxic amyloid-β (Aβ) production via inhibition of APP endocytosis. Internalized APP is delivered to endosomes and lysosomes where Aβ is produced. However, the molecular mechanism involved in the effect of APP O-GlcNAcylation on APP trafficking remains unknown. To investigate the relationship between APP O-GlcNAcylation and APP endocytosis, we tested the effects of insulin on neuroblastoma SH-SY5Y cells overexpressing APP and BACE1, and cultured rat hippocampal neurons. The present study showed that APP O-GlcNAcylation translocated APP from lipid raft to non-raft microdomains in the plasma membrane by using immunocytochemistry and discontinuous sucrose gradients method. By using the biotinylation method, we also found that APP preferentially underwent endocytosis from lipid rafts and that the amount of internalized APP from lipid rafts was specifically reduced by O-GlcNAcylation. These results indicate that O-GlcNAcylation can regulate lipid raft-dependent APP endocytosis via translocation of APP into non-raft microdomains. Our findings showed a new functional role of O-GlcNAcylation for the regulation of APP trafficking, offering new mechanistic insight for Aβ production. Full article
(This article belongs to the Special Issue Membrane Domains Organization and Interactions)
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18 pages, 2450 KiB  
Article
Tauroursodeoxycholic Acid (TUDCA)—Lipid Interactions and Antioxidant Properties of TUDCA Studied in Model of Photoreceptor Membranes
by Michał J. Sabat, Anna M. Wiśniewska-Becker, Michał Markiewicz, Katarzyna M. Marzec, Jakub Dybas, Justyna Furso, Paweł Pabisz, Mariusz Duda and Anna M. Pawlak
Membranes 2021, 11(5), 327; https://doi.org/10.3390/membranes11050327 - 29 Apr 2021
Cited by 3 | Viewed by 6242
Abstract
Tauroursodeoxycholic acid (TUDCA), a hydrophilic bile acid containing taurine conjugated with the ursodeoxycholic acid (UDCA), has been known and used from ancient times as a therapeutic compound in traditional Chinese medicine. TUDCA has recently been gaining significant interest as a neuroprotective agent, also [...] Read more.
Tauroursodeoxycholic acid (TUDCA), a hydrophilic bile acid containing taurine conjugated with the ursodeoxycholic acid (UDCA), has been known and used from ancient times as a therapeutic compound in traditional Chinese medicine. TUDCA has recently been gaining significant interest as a neuroprotective agent, also exploited in the visual disorders. Among several mechanisms of TUDCA’s protective action, its antioxidant activity and stabilizing effect on mitochondrial and plasma membranes are considered. In this work we investigated antioxidant activity of TUDCA and its impact on structural properties of model membranes of different composition using electron paramagnetic resonance spectroscopy and the spin labeling technique. Localization of TUDCA molecules in a pure POPC bilayer has been studied using a molecular dynamics simulation (MD). The obtained results indicate that TUDCA is not an efficient singlet oxygen (1O2 (1Δg)) quencher, and the determined rate constant of its interaction with 1O2 (1Δg) is only 1.9 × 105 M−1s−1. However, in lipid oxidation process induced by a Fenton reaction, TUDCA reveals substantial antioxidant activity significantly decreasing the rate of oxygen consumption in the system studied. In addition, TUDCA induces slight, but noticeable changes in the polarity and fluidity of the investigated model membranes. The results of performed MD simulation correspond very well with the experimental results. Full article
(This article belongs to the Special Issue Membrane Domains Organization and Interactions)
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8 pages, 1566 KiB  
Article
Condensing Effect of Cholesterol on hBest1/POPC and hBest1/SM Langmuir Monolayers
by Pavel Videv, Nikola Mladenov, Tonya Andreeva, Kirilka Mladenova, Veselina Moskova-Doumanova, Georgi Nikolaev, Svetla D. Petrova and Jordan A. Doumanov
Membranes 2021, 11(1), 52; https://doi.org/10.3390/membranes11010052 - 13 Jan 2021
Cited by 4 | Viewed by 1800
Abstract
Human bestrophin-1 protein (hBest1) is a transmembrane channel associated with the calcium-dependent transport of chloride ions in the retinal pigment epithelium as well as with the transport of glutamate and GABA in nerve cells. Interactions between hBest1, sphingomyelins, phosphatidylcholines and cholesterol are crucial [...] Read more.
Human bestrophin-1 protein (hBest1) is a transmembrane channel associated with the calcium-dependent transport of chloride ions in the retinal pigment epithelium as well as with the transport of glutamate and GABA in nerve cells. Interactions between hBest1, sphingomyelins, phosphatidylcholines and cholesterol are crucial for hBest1 association with cell membrane domains and its biological functions. As cholesterol plays a key role in the formation of lipid rafts, motional ordering of lipids and modeling/remodeling of the lateral membrane structure, we examined the effect of different cholesterol concentrations on the surface tension of hBest1/POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) and hBest1/SM Langmuir monolayers in the presence/absence of Ca2+ ions using surface pressure measurements and Brewster angle microscopy studies. Here, we report that cholesterol: (1) has negligible condensing effect on pure hBest1 monolayers detected mainly in the presence of Ca2+ ions, and; (2) induces a condensing effect on composite hBest1/POPC and hBest1/SM monolayers. These results offer evidence for the significance of intermolecular protein–lipid interactions for the conformational dynamics of hBest1 and its biological functions as multimeric ion channel. Full article
(This article belongs to the Special Issue Membrane Domains Organization and Interactions)
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Review

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18 pages, 1496 KiB  
Review
Misregulation of Wnt Signaling Pathways at the Plasma Membrane in Brain and Metabolic Diseases
by Mustafa Karabicici, Yagmur Azbazdar, Evin Iscan and Gunes Ozhan
Membranes 2021, 11(11), 844; https://doi.org/10.3390/membranes11110844 - 29 Oct 2021
Cited by 10 | Viewed by 3934
Abstract
Wnt signaling pathways constitute a group of signal transduction pathways that direct many physiological processes, such as development, growth, and differentiation. Dysregulation of these pathways is thus associated with many pathological processes, including neurodegenerative diseases, metabolic disorders, and cancer. At the same time, [...] Read more.
Wnt signaling pathways constitute a group of signal transduction pathways that direct many physiological processes, such as development, growth, and differentiation. Dysregulation of these pathways is thus associated with many pathological processes, including neurodegenerative diseases, metabolic disorders, and cancer. At the same time, alterations are observed in plasma membrane compositions, lipid organizations, and ordered membrane domains in brain and metabolic diseases that are associated with Wnt signaling pathway activation. Here, we discuss the relationships between plasma membrane components—specifically ligands, (co) receptors, and extracellular or membrane-associated modulators—to activate Wnt pathways in several brain and metabolic diseases. Thus, the Wnt–receptor complex can be targeted based on the composition and organization of the plasma membrane, in order to develop effective targeted therapy drugs. Full article
(This article belongs to the Special Issue Membrane Domains Organization and Interactions)
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21 pages, 903 KiB  
Review
Every Detail Matters. That Is, How the Interaction between Gα Proteins and Membrane Affects Their Function
by Agnieszka Polit, Paweł Mystek and Ewa Błasiak
Membranes 2021, 11(3), 222; https://doi.org/10.3390/membranes11030222 - 20 Mar 2021
Cited by 4 | Viewed by 2638
Abstract
In highly organized multicellular organisms such as humans, the functions of an individual cell are dependent on signal transduction through G protein-coupled receptors (GPCRs) and subsequently heterotrimeric G proteins. As most of the elements belonging to the signal transduction system are bound to [...] Read more.
In highly organized multicellular organisms such as humans, the functions of an individual cell are dependent on signal transduction through G protein-coupled receptors (GPCRs) and subsequently heterotrimeric G proteins. As most of the elements belonging to the signal transduction system are bound to lipid membranes, researchers are showing increasing interest in studying the accompanying protein–lipid interactions, which have been demonstrated to not only provide the environment but also regulate proper and efficient signal transduction. The mode of interaction between the cell membrane and G proteins is well known. Despite this, the recognition mechanisms at the molecular level and how the individual G protein-membrane attachment signals are interrelated in the process of the complex control of membrane targeting of G proteins remain unelucidated. This review focuses on the mechanisms by which mammalian Gα subunits of G proteins interact with lipids and the factors responsible for the specificity of membrane association. We summarize recent data on how these signaling proteins are precisely targeted to a specific site in the membrane region by introducing well-defined modifications as well as through the presence of polybasic regions within these proteins and interactions with other components of the heterocomplex. Full article
(This article belongs to the Special Issue Membrane Domains Organization and Interactions)
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