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Feature Papers in Biological Membrane Functions
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Feature Papers in Biological Membrane Functions

A topical collection in Membranes (ISSN 2077-0375). This collection belongs to the section "Biological Membrane Functions".

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Editors

Dr. Katia Cortese

E-Mail Website
Collection Editor
Department of Experimental Medicine (DIMES), Cellular Electron Microscopy Lab., University of Genoa, 16132 Genova, Italy
Interests: breast cancers; targeted therapies; cell biology; endocytosis and trafficking; autophagy; electron microscopy; light microscopy; HER2/ERBB2 receptor; lysosomes
Special Issues, Collections and Topics in MDPI journals
Dr. Jean Chemin

E-Mail Website
Collection Editor
Département de Neurosciences, Institut de Génomique Fonctionnelle, Centre National de la Recherche Scientifique, Unité Mixte de Recherche (UMR) 5203, Universités de Montpellier, 34094 Montpellier, France
Interests: ion channels; calcium channels; signal transduction; bioactive lipids; cannabinoids; sensory neurons; pain perception
Prof. Dr. Byung Joo Kim

E-Mail Website
Collection Editor
Division of Longevity and Biofunctional Medicine, School of Korean Medicine, Pusan National University, Yangsan 50612, Republic of Korea
Interests: ion channel; smooth muscle; gastrointestinal motility; apoptosis; interstitial cells of cajal
Prof. Dr. Rebecca J. Green

E-Mail Website
Collection Editor
Reading School of Pharmacy, University of Reading, Reading RG6 6DZ, UK
Interests: interactions with lipid membranes; antimicrobial peptides

Topical Collection Information

Dear Colleagues,

The field of biological membrane functions encompasses a diverse array of processes that are crucial for the functioning of living organisms. This topical collection of papers delves into the intricate mechanisms and key players involved in various aspects of membrane biology in health and disease. From ion channels to membrane fusion, each topic sheds light on fundamental processes that govern cellular dynamics and signal transduction. The collection aims to provide a comprehensive overview of the latest research findings and perspectives in this rapidly evolving field.

We look forward to receiving your outstanding contributions.

Dr. Katia Cortese
Dr. Jean Chemin
Prof. Dr. Byung Joo Kim
Prof. Dr. Rebecca J. Green
Collection 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 collection 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

  • ion channels
  • membrane transporters
  • membrane permeability
  • membrane trafficking processes
  • signal transduction
  • endocytosis
  • autophagy
  • membrane receptors
  • protein–membrane interactions
  • membrane fusion
  • membrane remodeling

Published Papers (3 papers)

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2024

Jump to: 2023

12 pages, 3746 KiB  
Article
The Helix Ring Peptide U11 from the Venom of the Ant, Tetramorium bicarinatum, Acts as a Putative Pore-Forming Toxin
by Steve Peigneur, Diogo Tibery and Jan Tytgat
Membranes 2024, 14(5), 114; https://doi.org/10.3390/membranes14050114 - 14 May 2024
Viewed by 175
Abstract
An insect neuroactive helix ring peptide called U11-MYRTX-Tb1a (abbreviated as U11) from the venom of the ant, Tetramorium bicarinatum. U11 is a 34-amino-acid peptide that is claimed to be one of the most paralytic peptides ever reported [...] Read more.
An insect neuroactive helix ring peptide called U11-MYRTX-Tb1a (abbreviated as U11) from the venom of the ant, Tetramorium bicarinatum. U11 is a 34-amino-acid peptide that is claimed to be one of the most paralytic peptides ever reported from ant venoms acting against blowflies and honeybees. The peptide features a compact triangular ring helix structure stabilized by a single disulfide bond, which is a unique three-dimensional scaffold among animal venoms. Pharmacological assays using Drosophila S2 cells have demonstrated that U11 is not cytotoxic but instead suggest that it may modulate potassium channels via the presence of a functional dyad. In our work described here, we have tested this hypothesis by investigating the action of synthetically made U11 on a wide array of voltage-gated K and Na channels since it is well known that these channels play a crucial role in the phenomenon of paralysis. Using the Xenopus laevis oocyte heterologous expression system and voltage clamp, our results have not shown any modulatory effect of 1 μM U11 on the activity of Kv1.1, Kv1.3, Kv1.4, Kv1.5, Shaker IR, Kv4.2, Kv7.1, Kv10.1, Kv11.1 and KQT1, nor on DmNav and BgNav. Instead, 10 μM U11 caused a quick and irreversible cytolytic effect, identical to the cytotoxic effect caused by Apis mellifera venom, which indicates that U11 can act as a pore-forming peptide. Interestingly, the paralytic dose (PD50) on blowflies and honeybees corresponds with the concentration at which U11 displays clear pore-forming activity. In conclusion, our results indicate that the insecticidal and paralytic effects caused by U11 may be explained by the putative pore formation of the peptide. Full article
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16 pages, 2817 KiB  
Article
An Untargeted Metabolomics Strategy to Identify Substrates of Known and Orphan E. coli Transporters
by Mohammad S. Radi, Lachlan J. Munro, Daniela Rago and Douglas B. Kell
Membranes 2024, 14(3), 70; https://doi.org/10.3390/membranes14030070 - 20 Mar 2024
Viewed by 1114
Abstract
Transport systems play a pivotal role in bacterial physiology and represent potential targets for medical and biotechnological applications. However, even in well-studied organisms like Escherichia coli, a notable proportion of transporters, exceeding as many as 30%, remain classified as orphans due to [...] Read more.
Transport systems play a pivotal role in bacterial physiology and represent potential targets for medical and biotechnological applications. However, even in well-studied organisms like Escherichia coli, a notable proportion of transporters, exceeding as many as 30%, remain classified as orphans due to their lack of known substrates. This study leveraged high-resolution LC-MS-based untargeted metabolomics to identify candidate substrates for these orphan transporters. Human serum, including a diverse array of biologically relevant molecules, served as an unbiased source for substrate exposure. The analysis encompassed 26 paired transporter mutant contrasts (i.e., knockout vs. overexpression), compared with the wild type, revealing distinct patterns of substrate uptake and excretion across various mutants. The convergence of candidate substrates across mutant scenarios provided robust validation, shedding light on novel transporter-substrate relationships, including those involving yeaV, hsrA, ydjE, and yddA. Furthermore, several substrates were contingent upon the specific mutants employed. This investigation underscores the utility of untargeted metabolomics for substrate identification in the absence of prior knowledge and lays the groundwork for subsequent validation experiments, holding significant implications for both medical and biotechnological advancements. Full article
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2023

Jump to: 2024

14 pages, 2750 KiB  
Article
Expression, Function and Trafficking of the Human ABCG2 Multidrug Transporter Containing Mutations in an Unstructured Cytoplasmic Loop
by Orsolya Mózner, Boglárka Zámbó, Zsuzsa Bartos, Anna Gergely, Kata Sára Szabó, Bálint Jezsó, Ágnes Telbisz, György Várady, László Homolya, Tamás Hegedűs and Balázs Sarkadi
Membranes 2023, 13(10), 822; https://doi.org/10.3390/membranes13100822 - 4 Oct 2023
Viewed by 1448
Abstract
The human ABCG2 multidrug transporter plays a crucial role in the absorption and excretion of xeno- and endobiotics, contributes to cancer drug resistance and the development of gout. In this work, we have analyzed the effects of selected variants, residing in a structurally [...] Read more.
The human ABCG2 multidrug transporter plays a crucial role in the absorption and excretion of xeno- and endobiotics, contributes to cancer drug resistance and the development of gout. In this work, we have analyzed the effects of selected variants, residing in a structurally unresolved cytoplasmic region (a.a. 354–367) of ABCG2 on the function and trafficking of this protein. A cluster of four lysines (K357–360) and the phosphorylation of a threonine (T362) residue in this region have been previously suggested to significantly affect the cellular fate of ABCG2. Here, we report that the naturally occurring K360del variant in human cells increased ABCG2 plasma membrane expression and accelerated cellular trafficking. The variable alanine replacements of the neighboring lysines had no significant effect on transport function, and the apical localization of ABCG2 in polarized cells has not been altered by any of these mutations. Moreover, in contrast to previous reports, we found that the phosphorylation-incompetent T362A, or the phosphorylation-mimicking T362E variants in this loop had no measurable effects on the function or expression of ABCG2. Molecular dynamics simulations indicated an increased mobility of the mutant variants with no major effects on the core structure of the protein. These results may help to decipher the potential role of this unstructured region within this transporter. Full article
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