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Membranes
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Molecular Mechanism of Cellular Membranes for Signal Transduction
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Molecular Mechanism of Cellular Membranes for Signal Transduction

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

Deadline for manuscript submissions: closed (20 December 2021) | Viewed by 19351

Special Issue Editor

Prof. Dr. Julia Schumann

E-Mail Website
Guest Editor
Clinic for Anesthesiology and Surgical Intensive Care, University Hospital Halle (Saale), 06120 Halle, Germany
Interests: endothelial dysfunction; macrophage–endothelial interaction; miRNAs; lipid rafts
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Cellular membranes are indispensable to life and play a pivotal role in cell functionality. An essential task of the membrane is to ensure cellular communication processes. It is known that the plasma membrane is composed of dynamic membrane patches, which differ in their assembly and biological activity. Formation of these microdomains, also referred to as lipid rafts, is thought to be due to unequal affinities between various lipid species. The domains have been shown to attract distinct proteins thereby promoting particular biochemical processes. In doing so the activity of cellular enzymes, transcription factors and post-transcriptional regulation factors (such as miRNAs) can be directly modulated.  It can thus be assumed that membrane microdomain structure influences cellular signal transduction and vice versa.

This Special Issue aims to cover the latest findings regarding membrane molecular assembly, signal transduction processes affecting membrane composition as well as the ways membranes impact on signalling cascades. Both original papers and reviews are welcome. Potential topics include, but are not limited to, the following:

  • Membrane (microdomain) architecture;
  • Mediators affecting membrane composition;
  • Assembly, localization, and interaction of membrane receptors;
  • Role of membrane microdomains for the initiation of signalling cascades;
  • Signal transduction processes influencing membrane functionality;
  • Impact of membrane-mediated signalling processes on post-transcriptional gene expression regulation

Prof. Dr. Julia Schumann
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 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

  • Membrane build-up
  • Lipid rafts
  • Membrane receptors
  • Signalling cascades
  • Transcriptional and post-transcriptional gene expression regulation

Published Papers (6 papers)

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Editorial

Jump to: Research, Review

2 pages, 188 KiB  
Editorial
Molecular Mechanism of Cellular Membranes for Signal Transduction
by Julia Schumann
Membranes 2022, 12(8), 748; https://doi.org/10.3390/membranes12080748 - 30 Jul 2022
Cited by 2 | Viewed by 971
Abstract
Membranes are central to cell function and crucial to life [...] Full article
(This article belongs to the Special Issue Molecular Mechanism of Cellular Membranes for Signal Transduction)

Research

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14 pages, 4300 KiB  
Article
Calmodulin-Dependent Regulation of Overexpressed but Not Endogenous TMEM16A Expressed in Airway Epithelial Cells
by Khaoula Talbi, Jiraporn Ousingsawat, Raquel Centeio, Rainer Schreiber and Karl Kunzelmann
Membranes 2021, 11(9), 723; https://doi.org/10.3390/membranes11090723 - 21 Sep 2021
Cited by 5 | Viewed by 1961
Abstract
Regulation of the Ca2+-activated Cl− channel TMEM16A by Ca2+/calmodulin (CAM) is discussed controversially. In the present study, we compared regulation of TMEM16A by Ca2+/calmodulin (holo-CAM), CAM-dependent kinase (CAMKII), and CAM-dependent phosphatase calcineurin in TMEM16A-overexpressing HEK293 cells [...] Read more.
Regulation of the Ca2+-activated Cl− channel TMEM16A by Ca2+/calmodulin (CAM) is discussed controversially. In the present study, we compared regulation of TMEM16A by Ca2+/calmodulin (holo-CAM), CAM-dependent kinase (CAMKII), and CAM-dependent phosphatase calcineurin in TMEM16A-overexpressing HEK293 cells and TMEM16A expressed endogenously in airway and colonic epithelial cells. The activator of the Ca2+/CAM-regulated K+ channel KCNN4, 1-EBIO, activated TMEM16A in overexpressing cells, but not in cells with endogenous expression of TMEM16A. Evidence is provided that CAM-interaction with TMEM16A modulates the Ca2+ sensitivity of the Cl− channel. Enhanced Ca2+ sensitivity of overexpressed TMEM16A explains its activity at basal (non-elevated) intracellular Ca2+ levels. The present results correspond well to a recent report that demonstrates a Ca2+-unbound form of CAM (apo-CAM) that is pre-associated with TMEM16A and mediates a Ca2+-dependent sensitization of activation (and inactivation). However, when using activators or inhibitors for holo-CAM, CAMKII, or calcineurin, we were unable to detect a significant impact of CAM, and limit evidence for regulation by CAM-dependent regulatory proteins on receptor-mediated activation of endogenous TMEM16A in airway or colonic epithelial cells. We propose that regulatory properties of TMEM16A and and other members of the TMEM16 family as detected in overexpression studies, should be validated for endogenous TMEM16A and physiological stimuli such as activation of phospholipase C (PLC)-coupled receptors. Full article
(This article belongs to the Special Issue Molecular Mechanism of Cellular Membranes for Signal Transduction)
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21 pages, 5006 KiB  
Article
Effective Perturbations of the Amplitude, Gating, and Hysteresis of IK(DR) Caused by PT-2385, an HIF-2α Inhibitor
by Hung-Tsung Hsiao, Guan-Ling Lu, Yen-Chin Liu and Sheng-Nan Wu
Membranes 2021, 11(8), 636; https://doi.org/10.3390/membranes11080636 - 17 Aug 2021
Cited by 5 | Viewed by 2441
Abstract
PT-2385 is currently regarded as a potent and selective inhibitor of hypoxia-inducible factor-2α (HIF-2α), with potential antineoplastic activity. However, the membrane ion channels changed by this compound are obscure, although it is reasonable to assume that the compound might act on surface membrane [...] Read more.
PT-2385 is currently regarded as a potent and selective inhibitor of hypoxia-inducible factor-2α (HIF-2α), with potential antineoplastic activity. However, the membrane ion channels changed by this compound are obscure, although it is reasonable to assume that the compound might act on surface membrane before entering the cell´s interior. In this study, we intended to explore whether it and related compounds make any adjustments to the plasmalemmal ionic currents of pituitary tumor (GH3) cells and human 13-06-MG glioma cells. Cell exposure to PT-2385 suppressed the peak or late amplitude of delayed-rectifier K+ current (IK(DR)) in a time- and concentration-dependent manner, with IC50 values of 8.1 or 2.2 µM, respectively, while the KD value in PT-2385-induced shortening in the slow component of IK(DR) inactivation was estimated to be 2.9 µM. The PT-2385-mediated block of IK(DR) in GH3 cells was little-affected by the further application of diazoxide, cilostazol, or sorafenib. Increasing PT-2385 concentrations shifted the steady-state inactivation curve of IK(DR) towards a more hyperpolarized potential, with no change in the gating charge of the current, and also prolonged the time-dependent recovery of the IK(DR) block. The hysteretic strength of IK(DR) elicited by upright or inverted isosceles-triangular ramp voltage was decreased during exposure to PT-2385; meanwhile, the activation energy involved in the gating of IK(DR) elicitation was noticeably raised in its presence. Alternatively, the presence of PT-2385 in human 13-06-MG glioma cells effectively decreased the amplitude of IK(DR). Considering all of the experimental results together, the effects of PT-2385 on ionic currents demonstrated herein could be non-canonical and tend to be upstream of the inhibition of HIF-2α. This action therefore probably contributes to down-streaming mechanisms through the changes that it or other structurally resemblant compounds lead to in the perturbations of the functional activities of pituitary cells or neoplastic astrocytes, in the case that in vivo observations occur. Full article
(This article belongs to the Special Issue Molecular Mechanism of Cellular Membranes for Signal Transduction)
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23 pages, 3304 KiB  
Article
Phosphorylation of mRNA-Binding Proteins Puf1 and Puf2 by TORC2-Activated Protein Kinase Ypk1 Alleviates Their Repressive Effects
by Henri A. Galez, Françoise M. Roelants, Sarah M. Palm, Kendra K. Reynaud, Nicholas T. Ingolia and Jeremy Thorner
Membranes 2021, 11(7), 500; https://doi.org/10.3390/membranes11070500 - 30 Jun 2021
Cited by 3 | Viewed by 3170
Abstract
Members of the Puf family of RNA-binding proteins typically associate via their Pumilio homology domain with specific short motifs in the 3’-UTR of an mRNA and thereby influence the stability, localization and/or efficiency of translation of the bound transcript. In our prior unbiased [...] Read more.
Members of the Puf family of RNA-binding proteins typically associate via their Pumilio homology domain with specific short motifs in the 3’-UTR of an mRNA and thereby influence the stability, localization and/or efficiency of translation of the bound transcript. In our prior unbiased proteome-wide screen for targets of the TORC2-stimulated protein kinase Ypk1, we identified the paralogs Puf1/Jsn1 and Puf2 as high-confidence substrates. Earlier work by others had demonstrated that Puf1 and Puf2 exhibit a marked preference for interaction with mRNAs encoding plasma membrane-associated proteins, consistent with our previous studies documenting that a primary physiological role of TORC2-Ypk1 signaling is maintenance of plasma membrane homeostasis. Here, we show, first, that both Puf1 and Puf2 are authentic Ypk1 substrates both in vitro and in vivo. Fluorescently tagged Puf1 localizes constitutively in cortical puncta closely apposed to the plasma membrane, whereas Puf2 does so in the absence of its Ypk1 phosphorylation, but is dispersed in the cytosol when phosphorylated. We further demonstrate that Ypk1-mediated phosphorylation of Puf1 and Puf2 upregulates production of the protein products of the transcripts to which they bind, with a concomitant increase in the level of the cognate mRNAs. Thus, Ypk1 phosphorylation relieves Puf1- and Puf2-mediated post-transcriptional repression mainly by counteracting their negative effect on transcript stability. Using a heterologous protein-RNA tethering and fluorescent protein reporter assay, the consequence of Ypk1 phosphorylation in vivo was recapitulated for full-length Puf1 and even for N-terminal fragments (residues 1-340 and 143-295) corresponding to the region upstream of its dimerization domain (an RNA-recognition motif fold) encompassing its two Ypk1 phosphorylation sites (both also conserved in Puf2). This latter result suggests that alleviation of Puf1-imposed transcript destabilization does not obligatorily require dissociation of Ypk1-phosphorylated Puf1 from a transcript. Our findings add new insight about how the TORC2-Ypk1 signaling axis regulates the content of plasma membrane-associated proteins to promote maintenance of the integrity of the cell envelope. Full article
(This article belongs to the Special Issue Molecular Mechanism of Cellular Membranes for Signal Transduction)
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Review

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26 pages, 20613 KiB  
Review
Platelet Membrane: An Outstanding Factor in Cancer Metastasis
by Nazly Z. Durán-Saenz, Alejandra Serrano-Puente, Perla I. Gallegos-Flores, Brenda D. Mendoza-Almanza, Edgar L. Esparza-Ibarra, Susana Godina-González, Irma E. González-Curiel, Jorge L. Ayala-Luján, Marisa Hernández-Barrales, Cecilia F. Cueto-Villalobos, Sharahy Y. Frausto-Fierros, Luis A. Burciaga-Hernandez and Gretel Mendoza-Almanza
Membranes 2022, 12(2), 182; https://doi.org/10.3390/membranes12020182 - 3 Feb 2022
Cited by 6 | Viewed by 5428
Abstract
In addition to being biological barriers where the internalization or release of biomolecules is decided, cell membranes are contact structures between the interior and exterior of the cell. Here, the processes of cell signaling mediated by receptors, ions, hormones, cytokines, enzymes, growth factors, [...] Read more.
In addition to being biological barriers where the internalization or release of biomolecules is decided, cell membranes are contact structures between the interior and exterior of the cell. Here, the processes of cell signaling mediated by receptors, ions, hormones, cytokines, enzymes, growth factors, extracellular matrix (ECM), and vesicles begin. They triggering several responses from the cell membrane that include rearranging its components according to the immediate needs of the cell, for example, in the membrane of platelets, the formation of filopodia and lamellipodia as a tissue repair response. In cancer, the cancer cells must adapt to the new tumor microenvironment (TME) and acquire capacities in the cell membrane to transform their shape, such as in the case of epithelial−mesenchymal transition (EMT) in the metastatic process. The cancer cells must also attract allies in this challenging process, such as platelets, fibroblasts associated with cancer (CAF), stromal cells, adipocytes, and the extracellular matrix itself, which limits tumor growth. The platelets are enucleated cells with fairly interesting growth factors, proangiogenic factors, cytokines, mRNA, and proteins, which support the development of a tumor microenvironment and support the metastatic process. This review will discuss the different actions that platelet membranes and cancer cell membranes carry out during their relationship in the tumor microenvironment and metastasis. Full article
(This article belongs to the Special Issue Molecular Mechanism of Cellular Membranes for Signal Transduction)
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18 pages, 1636 KiB  
Review
Lipid Transporters Beam Signals from Cell Membranes
by Miliça Ristovski, Danny Farhat, Shelly Ellaine M. Bancud and Jyh-Yeuan Lee
Membranes 2021, 11(8), 562; https://doi.org/10.3390/membranes11080562 - 26 Jul 2021
Cited by 7 | Viewed by 4311
Abstract
Lipid composition in cellular membranes plays an important role in maintaining the structural integrity of cells and in regulating cellular signaling that controls functions of both membrane-anchored and cytoplasmic proteins. ATP-dependent ABC and P4-ATPase lipid transporters, two integral membrane proteins, are known to [...] Read more.
Lipid composition in cellular membranes plays an important role in maintaining the structural integrity of cells and in regulating cellular signaling that controls functions of both membrane-anchored and cytoplasmic proteins. ATP-dependent ABC and P4-ATPase lipid transporters, two integral membrane proteins, are known to contribute to lipid translocation across the lipid bilayers on the cellular membranes. In this review, we will highlight current knowledge about the role of cholesterol and phospholipids of cellular membranes in regulating cell signaling and how lipid transporters participate this process. Full article
(This article belongs to the Special Issue Molecular Mechanism of Cellular Membranes for Signal Transduction)
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