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Special Issue "Channels and Transporters in Cells and Tissues 2.0"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (31 December 2020).

Special Issue Editor

Dr. Graça Soveral
E-Mail Website
Guest Editor
Faculdade de Farmacia, Universidaded de Lisboa, Research Institute for Medicines (iMed.ULisboa), Lisbon, Portugal
Interests: water and solute transport; transporter; channel; metabolism; diseases
Special Issues and Collections in MDPI journals

Special Issue Information

Dear Colleagues,

Channels and transporters are membrane proteins that mediate the traffic of water, ions, and solutes across biological membranes, and are crucial to maintaining homeostasis assuring cell survival upon intracellular or environmental stress. The absence or dysfunction of channels and transporters may have dramatic consequences for cellular and tissue function and cause disease. Thus, the mechanisms of physiological regulation and chemical modulation of membrane proteins are an emergent topic in the fields of biology, agriculture, and medicine that present opportunities for drug discovery and new therapies.

This Special Issue “Channels and Transporters in Cells and Tissues 2.0” will still focus on the function and regulation of membrane transport proteins across all living organisms, including their potential use as drug targets. Authors are invited to submit original research and review papers addressing the topic of this Special Issue.

Prof. Graça Soveral
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 papers will be 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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • Membrane transport and regulation;
  • Structure–function relationship;
  • Water, ions, and solutes transportation;
  • Membrane permeability;
  • Osmoregulation;
  • Chemical modulation;
  • Therapeutic applications;
  • Drug discovery;
  • Disease;
  • Prokaryotic and eukaryotic cells.

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Published Papers (7 papers)

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Research

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Open AccessArticle
Modulation of Actin Filament Dynamics by Inward Rectifying of Potassium Channel Kir2.1
Int. J. Mol. Sci. 2020, 21(20), 7479; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21207479 - 10 Oct 2020
Viewed by 566
Abstract
Apart from its ion channel properties, the Kir2.1 channel has been found in tumors and cancer cells to facilitate cancer cell motility. It is assumed that Kir2.1 might be associated with cell actin filament dynamics. With the help of structured illumination microscopy (SIM), [...] Read more.
Apart from its ion channel properties, the Kir2.1 channel has been found in tumors and cancer cells to facilitate cancer cell motility. It is assumed that Kir2.1 might be associated with cell actin filament dynamics. With the help of structured illumination microscopy (SIM), we show that Kir2.1 overexpression promotes actin filament dynamics, cell invasion, and adhesion. Mutated Kir2.1 channels, with impaired membrane expression, present much weaker actin regulatory effects, which indicates that precise Kir2.1 membrane localization is key to its actin filament remolding effect. It is found that Kir2.1 membrane expression and anchoring are associated with PIP2 affinity, and PIP2 depletion inhibits actin filament dynamics. We also report that membrane-expressed Kir2.1 regulates redistribution and phosphorylation of FLNA (filamin A), which may be the mechanism underlying Kir2.1 and actin filament dynamics. In conclusion, Kir2.1 membrane localization regulates cell actin filaments, and not the ion channel properties. These data indicate that Kir2.1 may have additional cellular functions distinct from the regulation of excitability, which provides new insight into the study of channel proteins. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissues 2.0)
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Open AccessArticle
Insights into the Selectivity Mechanisms of Grapevine NIP Aquaporins
Int. J. Mol. Sci. 2020, 21(18), 6697; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21186697 - 13 Sep 2020
Cited by 1 | Viewed by 747
Abstract
Nodulin 26-like intrinsic proteins (NIPs) of the plant aquaporin family majorly facilitate the transport of physiologically relevant solutes. The present study intended to investigate how substrate selectivity in grapevine NIPs is influenced by the aromatic/arginine (ar/R) selectivity filter within the pore and the [...] Read more.
Nodulin 26-like intrinsic proteins (NIPs) of the plant aquaporin family majorly facilitate the transport of physiologically relevant solutes. The present study intended to investigate how substrate selectivity in grapevine NIPs is influenced by the aromatic/arginine (ar/R) selectivity filter within the pore and the possible underlying mechanisms. A mutational approach was used to interchange the ar/R residues between grapevine NIPs (VvTnNIP1;1 with VvTnNIP6;1, and VvTnNIP2;1 with VvTnNIP5;1). Their functional characterization by stopped-flow spectroscopy in Saccharomyces cerevisiae revealed that mutations in residues of H2/H5 helices in VvTnNIP1;1 and VvTnNIP6;1 caused a general decline in membrane glycerol permeability but did not impart the expected substrate conductivity in the mutants. This result suggests that ar/R filter substitution could alter the NIP channel activity, but it was not sufficient to interchange their substrate preferences. Further, homology modeling analyses evidenced that variations in the pore radius combined with the differences in the channel’s physicochemical properties (hydrophilicity/hydrophobicity) may drive substrate selectivity. Furthermore, yeast growth assays showed that H5 residue substitution alleviated the sensitivity of VvTnNIP2;1 and VvTnNIP5;1 to As, B, and Se, implying importance of H5 sequence for substrate selection. These results contribute to the knowledge of the overall determinants of substrate selectivity in NIPs. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissues 2.0)
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Open AccessArticle
A Mechanosensitive Channel, Mouse Transmembrane Channel-Like Protein 1 (mTMC1) Is Translated from a Splice Variant mTmc1ex1 but Not from the Other Variant mTmc1ex2
Int. J. Mol. Sci. 2020, 21(18), 6465; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21186465 - 04 Sep 2020
Cited by 1 | Viewed by 602
Abstract
Mechanical stimuli caused by sound waves are detected by hair cells in the cochlea through the opening of mechanoelectrical transduction (MET) channels. Transmembrane channel-like protein 1 (TMC1) has been revealed to be the pore-forming component of the MET channel. The two splice variants [...] Read more.
Mechanical stimuli caused by sound waves are detected by hair cells in the cochlea through the opening of mechanoelectrical transduction (MET) channels. Transmembrane channel-like protein 1 (TMC1) has been revealed to be the pore-forming component of the MET channel. The two splice variants for mouse Tmc1 (mTmc1ex1 and mTmc1ex2) were reported to be expressed in the cochlea of infant mice, though only the sequence of mTmc1ex2 had been deposited in GenBank. However, due to the presence of an upstream open reading frame (uORF) and the absence of a typical Kozak sequence in mTmc1ex2, we questioned whether mTMC1 was translated from mTmc1ex2. Therefore, in this study, we evaluated which splice variant was protein-coding mRNA. Firstly, the results of RT-PCR and cDNA cloning of mTmc1 using mRNA isolated from the cochlea of five-week-old mice suggested that more Tmc1ex1 were expressed than mTmc1ex2. Secondly, mTMC1 was translated from mTmc1ex1 but not from mTmc1ex2 in a heterologous expression system. Finally, analyses using site-directed mutagenesis revealed that the uORF and the weak Kozak sequence in mTmc1ex2 prevented the translation of mTMC1 from mTmc1ex2. These results suggest that mTmc1ex1 plays a main role in the expression of mTMC1 in the mouse cochlea, and therefore, mTmc1ex1 should be the mRNA for mTMC1 hereafter. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissues 2.0)
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Open AccessArticle
Sweet Cherry (Prunus avium L.) PaPIP1;4 Is a Functional Aquaporin Upregulated by Pre-Harvest Calcium Treatments that Prevent Cracking
Int. J. Mol. Sci. 2020, 21(8), 3017; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21083017 - 24 Apr 2020
Cited by 1 | Viewed by 962
Abstract
The involvement of aquaporins in rain-induced sweet cherry (Prunus avium L.) fruit cracking is an important research topic with potential agricultural applications. In the present study, we performed the functional characterization of PaPIP1;4, the most expressed aquaporin in sweet cherry fruit. Field [...] Read more.
The involvement of aquaporins in rain-induced sweet cherry (Prunus avium L.) fruit cracking is an important research topic with potential agricultural applications. In the present study, we performed the functional characterization of PaPIP1;4, the most expressed aquaporin in sweet cherry fruit. Field experiments focused on the pre-harvest exogenous application to sweet cherry trees, cultivar Skeena, with a solution of 0.5% CaCl2, which is the most common treatment to prevent cracking. Results show that PaPIP1;4 was mostly expressed in the fruit peduncle, but its steady-state transcript levels were higher in fruits from CaCl2-treated plants than in controls. The transient expression of PaPIP1;4-GFP in tobacco epidermal cells and the overexpression of PaPIP1;4 in YSH1172 yeast mutation showed that PaPIP1;4 is a plasma membrane protein able to transport water and hydrogen peroxide. In this study, we characterized for the first time a plasma membrane sweet cherry aquaporin able to transport water and H2O2 that is upregulated by the pre-harvest exogenous application of CaCl2 supplements. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissues 2.0)
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Review

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Open AccessReview
Current Understanding of Role of Vesicular Transport in Salt Secretion by Salt Glands in Recretohalophytes
Int. J. Mol. Sci. 2021, 22(4), 2203; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22042203 - 23 Feb 2021
Viewed by 324
Abstract
Soil salinization is a serious and growing problem around the world. Some plants, recognized as the recretohalophytes, can normally grow on saline–alkali soil without adverse effects by secreting excessive salt out of the body. The elucidation of the salt secretion process is of [...] Read more.
Soil salinization is a serious and growing problem around the world. Some plants, recognized as the recretohalophytes, can normally grow on saline–alkali soil without adverse effects by secreting excessive salt out of the body. The elucidation of the salt secretion process is of great significance for understanding the salt tolerance mechanism adopted by the recretohalophytes. Between the 1950s and the 1970s, three hypotheses, including the osmotic potential hypothesis, the transfer system similar to liquid flow in animals, and vesicle-mediated exocytosis, were proposed to explain the salt secretion process of plant salt glands. More recently, increasing evidence has indicated that vesicular transport plays vital roles in salt secretion of recretohalophytes. Here, we summarize recent findings, especially regarding the molecular evidence on the functional roles of vesicular trafficking in the salt secretion process of plant salt glands. A model of salt secretion in salt gland is also proposed. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissues 2.0)
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Open AccessReview
Aquaporins in Immune Cells and Inflammation: New Targets for Drug Development
Int. J. Mol. Sci. 2021, 22(4), 1845; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22041845 - 12 Feb 2021
Viewed by 393
Abstract
The mammalian immune system senses foreign antigens by mechanisms that involve the interplay of various kinds of immune cells, culminating in inflammation resolution and tissue clearance. The ability of the immune cells to communicate (via chemokines) and to shift shape for migration, phagocytosis [...] Read more.
The mammalian immune system senses foreign antigens by mechanisms that involve the interplay of various kinds of immune cells, culminating in inflammation resolution and tissue clearance. The ability of the immune cells to communicate (via chemokines) and to shift shape for migration, phagocytosis or antigen uptake is mainly supported by critical proteins such as aquaporins (AQPs) that regulate water fluid homeostasis and volume changes. AQPs are protein channels that facilitate water and small uncharged molecules’ (such as glycerol or hydrogen peroxide) diffusion through membranes. A number of AQP isoforms were found upregulated in inflammatory conditions and are considered essential for the migration and survival of immune cells. The present review updates information on AQPs’ involvement in immunity and inflammatory processes, highlighting their role as crucial players and promising targets for drug discovery. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissues 2.0)
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Open AccessReview
The Role of Ca2+-NFATc1 Signaling and Its Modulation on Osteoclastogenesis
Int. J. Mol. Sci. 2020, 21(10), 3646; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21103646 - 21 May 2020
Cited by 3 | Viewed by 805
Abstract
The increasing of intracellular calcium concentration is a fundamental process for mediating osteoclastogenesis, which is involved in osteoclastic bone resorption. Cytosolic calcium binds to calmodulin and subsequently activates calcineurin, leading to NFATc1 activation, a master transcription factor required for osteoclast differentiation. Targeting the [...] Read more.
The increasing of intracellular calcium concentration is a fundamental process for mediating osteoclastogenesis, which is involved in osteoclastic bone resorption. Cytosolic calcium binds to calmodulin and subsequently activates calcineurin, leading to NFATc1 activation, a master transcription factor required for osteoclast differentiation. Targeting the various activation processes in osteoclastogenesis provides various therapeutic strategies for bone loss. Diverse compounds that modulate calcium signaling have been applied to regulate osteoclast differentiation and, subsequently, attenuate bone loss. Thus, in this review, we summarized the modulation of the NFATc1 pathway through various compounds that regulate calcium signaling and the calcium influx machinery. Furthermore, we addressed the involvement of transient receptor potential channels in osteoclastogenesis. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissues 2.0)
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