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Biomolecules
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Defects in the Transport Mechanism of Membrane Proteins and Related...
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Defects in the Transport Mechanism of Membrane Proteins and Related Diseases, 2nd Edition

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Cellular Biochemistry".

Deadline for manuscript submissions: 10 June 2026 | Viewed by 5012

Special Issue Editor

Dr. Daniela Valeria Miniero

E-Mail Website
Guest Editor
Department of Medicine and Surgery, LUM University Giuseppe Degennaro Torre Rossi, 70010 Casamassima, Italy
Interests: structure/function relationship; transport mechanism; mitochondrial transport proteins; mitochondrial carrier diseases; mitochondrial carrier identification; design, synthesis and biological evaluation of new drugs against neurodegenerative diseases

Special Issue Information

Dear Colleagues,

Following a very successful first run, we are pleased to announce the launch of the second edition of a Special Issue on ‘Defects in the Transport Mechanism of Membrane Proteins and Related Diseases’.

Membrane transport proteins play crucial roles across biological membranes and participate in cell physiology, metabolism and signaling, maintaining cellular homeostasis, and permitting the translocation of many classes of metabolites (i.e., sugar, amino acids, lipids, vitamins, inorganic ions and others). These proteins are essential for cellular functions ensuring cell survival in response to frequent stimuli of intracellular or environmental stress. Indeed, the transport mechanism exerted by membrane transport proteins, generating concentration gradients via active transport mechanisms, passive diffusion and ion channels, contributes to the regulation of biochemical pathways through correct cellular concentrations of substrates and products. Therefore, genetic mutations or the impairment of transport systems would turn out in defects in the transport mechanism with changes in the expression, activity and structure of proteins, which are manifested in different groups of neurodegenerative and metabolic diseases.

Hence, the purpose of this Special Issue “Defects in the Transport Mechanism of Membrane Proteins and Related Diseases" is to integrate current knowledge regarding physiological functions and the mechanisms of transport of a wide group of membrane transport proteins underlying their involvements in the initiation and progression of many diseases. Research papers and review manuscripts depicting a special focus on membrane transporters are invited for submission. Short communications will also be taken into consideration.

Dr. Daniela Valeria Miniero
Guest Editor

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 250 words) can be sent to the Editorial Office for assessment.

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. Biomolecules 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

  • function, structure and folding of membrane transport proteins
  • pathological mutations
  • mechanism of transport
  • neurological and metabolic disease
  • transport of nanoparticles
  • organelle membranes
  • cellular function and signaling
  • bioenergetics
  • neuroinflammation
  • nanoformulations for drug targets

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Related Special Issue

Published Papers (3 papers)

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Review

18 pages, 1383 KB  
Review
Intrinsic Asymmetry in Weak Acid Transmembrane Transporters
by Emmi Jaeger, Sebastian Buss and Eric Beitz
Biomolecules 2026, 16(1), 91; https://doi.org/10.3390/biom16010091 - 6 Jan 2026
Viewed by 836
Abstract
Transmembrane facilitation of substrates by channels and secondary active transporters results in a defined steady-state concentration ratio across the membrane. Evidence is accumulating that asymmetry in the structural build of the transporters, or interaction with asymmetric partner proteins, can shift the position of [...] Read more.
Transmembrane facilitation of substrates by channels and secondary active transporters results in a defined steady-state concentration ratio across the membrane. Evidence is accumulating that asymmetry in the structural build of the transporters, or interaction with asymmetric partner proteins, can shift the position of the transmembrane equilibrium by biased transport directionality. For instance, the bacterial lactose transporter, LacY, and two amino acid transporters, i.e., the human excitatory amino acid carrier, EAAC1, and the yeast lysine permease, Lyp1, were reported to exhibit distinct transport kinetics in the inward and outward direction by protein-intrinsic properties. A recent example is transport modulation of human monocarboxylate transporters, MCT, by shedding of the extracellular domain of an ancillary protein, basigin. Loss of the domain selectively increases export of lactate from lung cancer cells by a factor of four, contributing to the Warburg effect and malignancy. Further, intrinsic properties of monocarboxylate transporters involving asymmetric affinities of substrate binding, or biased open probabilities were shown to generate preference for one transport direction. Here, we discuss molecular mechanisms and physiological contexts of asymmetric secondary active transmembrane transport. Focus is laid on experimentally established cases, and examples are given in which putative bias in transport directionality may have been overlooked. Full article
(This article belongs to the Special Issue Defects in the Transport Mechanism of Membrane Proteins and Related Diseases, 2nd Edition)
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33 pages, 3359 KB  
Review
Human CTR1 Through the Ages: Milestones and Emerging Roles in Disease and Therapy
by Shahaf Peleg, Lukas Hofmann and Sharon Ruthstein
Biomolecules 2025, 15(12), 1739; https://doi.org/10.3390/biom15121739 - 15 Dec 2025
Viewed by 1252
Abstract
Copper transporter 1 (CTR1) is the primary high affinity importer for Cu(I) in eukaryotic cells. CTR1 plays an essential role in maintaining copper homeostasis which is crucial for diverse biological processes. Since its discovery in 1997, research on human CTR1 (hCTR1) has progressed [...] Read more.
Copper transporter 1 (CTR1) is the primary high affinity importer for Cu(I) in eukaryotic cells. CTR1 plays an essential role in maintaining copper homeostasis which is crucial for diverse biological processes. Since its discovery in 1997, research on human CTR1 (hCTR1) has progressed from foundational biochemical characterization to detailed structural and functional elucidation, expanding our understanding of its involvement in human diseases. Here we summarize the current understanding of hCTR1, including its structural features, copper-binding motifs, regulation, trafficking pathways, and roles in disease. We also highlight emerging evidence implicating hCTR1 in cancer, neurodegenerative disorders, and inherited copper metabolism syndromes, emphasizing its potential as a therapeutic target and drug delivery facilitator. Finally, we discuss recent studies and outline future directions, aimed at fully harnessing the biomedical potential of hCTR1. Full article
(This article belongs to the Special Issue Defects in the Transport Mechanism of Membrane Proteins and Related Diseases, 2nd Edition)
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Graphical abstract

23 pages, 2433 KB  
Review
Massive Activation of GABAA Receptors: Rundown, Ionic and Neurodegenerative Consequences
by Sergey A. Menzikov, Danila M. Zaichenko, Aleksey A. Moskovtsev, Sergey G. Morozov and Aslan A. Kubatiev
Biomolecules 2025, 15(7), 1003; https://doi.org/10.3390/biom15071003 - 13 Jul 2025
Cited by 2 | Viewed by 2454
Abstract
The GABAA receptors, through a short-term interaction with a mediator, induce hyperpolarization of the membrane potential (Vm) via the passive influx of chloride ions (Cl−) into neurons. The massive (or intense) activation of the GABAARs [...] Read more.
The GABAA receptors, through a short-term interaction with a mediator, induce hyperpolarization of the membrane potential (Vm) via the passive influx of chloride ions (Cl−) into neurons. The massive (or intense) activation of the GABAARs by the agonist could potentially lead to depolarization/excitation of the Vm. Although the ionic mechanisms of GABAA-mediated depolarization remain incompletely understood, a combination of the outward chloride current and the inward bicarbonate current and the resulting pH shift are the main reasons for this event. The GABAA responses are determined by the ionic gradients—neuronal pH/bicarbonate homeostasis is maintained by carbonic anhydrase and electroneutral/electrogenic bicarbonate transporters and the chloride level is maintained by secondary active cation–chloride cotransporters. Massive activation can also induce the rundown effect of the receptor function. This rundown effect partly involves phosphorylation, Ca2+ and the processes of receptor desensitization. In addition, by various methods (including fluorescence and optical genetic methods), it has been shown that massive activation of GABAARs during pathophysiological activity is also associated with an increase in [Cl−]i and a decline in the pH and ATP levels in neurons. Although the relationship between the neuronal changes induced by massive activation of GABAergic signaling and the risk of developing neurodegenerative disease has been extensively studied, the molecular determinants of this process remain somewhat mysterious. The aim of this review is to summarize the data on the relationship between the massive activation of inhibitory signaling and the ionic changes in neurons. The potential role of receptor dysfunction during massive activation and the resulting ionic and metabolic disruption in neurons during the manifestation of network/seizure activity will be considered. Full article
(This article belongs to the Special Issue Defects in the Transport Mechanism of Membrane Proteins and Related Diseases, 2nd Edition)
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