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Raft Microdomains and Cell Signaling
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Raft Microdomains and Cell Signaling

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

Deadline for manuscript submissions: closed (30 June 2021) | Viewed by 23121

Special Issue Editor

Dr. Jean-Pierre Jaffrézou

E-Mail Website
Guest Editor
CNRS UMR5549, CerCo, TMBI, CHU Purpan, Pavillon Baudot, 31059 Toulouse, France
Interests: cancer therapies; chemoresistance; microdomains; cell signaling
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

A model for membrane structure that describes the organization of the lipid microdomains as platforms (or rafts) is emerging as an important factor in a variety of cellular processes. Proteins can selectively be included or excluded from these microdomains, which can serve as relay stations in intracellular signaling. The main forces driving the formation of rafts are lipid–lipid interactions, dependent on the biophysical characteristics of the lipid components.

This Special Issue will discuss the recent advances in the field of raft microdomains, thereby contributing to our knowledge on how the selective inclusion or exclusion of key signaling molecules within raft microdomains play a role in signal transduction and many other cellular events.

Dr. Jean-Pierre Jaffrézou
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. 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

  • Lipid rafts
  • Sphingolipids
  • Cell signaling
  • Stress
  • Cell death
  • Lipid–protein interaction
  • Model membranes
  • Membrane protein diffusion
  • Raft structure and dynamics
  • Membrane partitioning

Published Papers (6 papers)

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Research

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15 pages, 2448 KiB  
Article
Quantitative FRET Microscopy Reveals a Crucial Role of Cytoskeleton in Promoting PI(4,5)P2 Confinement
by Maria J. Sarmento, Luís Borges-Araújo, Sandra N. Pinto, Nuno Bernardes, Joana C. Ricardo, Ana Coutinho, Manuel Prieto and Fábio Fernandes
Int. J. Mol. Sci. 2021, 22(21), 11727; https://doi.org/10.3390/ijms222111727 - 29 Oct 2021
Cited by 1 | Viewed by 2350
Abstract
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is an essential plasma membrane component involved in several cellular functions, including membrane trafficking and cytoskeleton organization. This function multiplicity is partially achieved through a dynamic spatiotemporal organization of PI(4,5)P2 within the membrane. Here, we use a [...] Read more.
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is an essential plasma membrane component involved in several cellular functions, including membrane trafficking and cytoskeleton organization. This function multiplicity is partially achieved through a dynamic spatiotemporal organization of PI(4,5)P2 within the membrane. Here, we use a Förster resonance energy transfer (FRET) approach to quantitatively assess the extent of PI(4,5)P2 confinement within the plasma membrane. This methodology relies on the rigorous evaluation of the dependence of absolute FRET efficiencies between pleckstrin homology domains (PHPLCδ) fused with fluorescent proteins and their average fluorescence intensity at the membrane. PI(4,5)P2 is found to be significantly compartmentalized at the plasma membrane of HeLa cells, and these clusters are not cholesterol-dependent, suggesting that membrane rafts are not involved in the formation of these nanodomains. On the other hand, upon inhibition of actin polymerization, compartmentalization of PI(4,5)P2 is almost entirely eliminated, showing that the cytoskeleton network is the critical component responsible for the formation of nanoscale PI(4,5)P2 domains in HeLa cells. Full article
(This article belongs to the Special Issue Raft Microdomains and Cell Signaling)
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22 pages, 7348 KiB  
Article
Binding of Amyloid β(1–42)-Calmodulin Complexes to Plasma Membrane Lipid Rafts in Cerebellar Granule Neurons Alters Resting Cytosolic Calcium Homeostasis
by Joana Poejo, Jairo Salazar, Ana M. Mata and Carlos Gutierrez-Merino
Int. J. Mol. Sci. 2021, 22(4), 1984; https://doi.org/10.3390/ijms22041984 - 17 Feb 2021
Cited by 13 | Viewed by 1818
Abstract
Lipid rafts are a primary target in studies of amyloid β (Aβ) cytotoxicity in neurons. Exogenous Aβ peptides bind to lipid rafts, which in turn play a key role in Aβ uptake, leading to the formation of neurotoxic intracellular Aβ aggregates. On the [...] Read more.
Lipid rafts are a primary target in studies of amyloid β (Aβ) cytotoxicity in neurons. Exogenous Aβ peptides bind to lipid rafts, which in turn play a key role in Aβ uptake, leading to the formation of neurotoxic intracellular Aβ aggregates. On the other hand, dysregulation of intracellular calcium homeostasis in neurons has been observed in Alzheimer’s disease (AD). In a previous work, we showed that Aβ(1–42), the prevalent Aβ peptide found in the amyloid plaques of AD patients, binds with high affinity to purified calmodulin (CaM), with a dissociation constant ≈1 nM. In this work, to experimentally assess the Aβ(1–42) binding capacity to intracellular CaM, we used primary cultures of mature cerebellar granule neurons (CGN) as a neuronal model. Our results showed a large complexation of submicromolar concentrations of Aβ(1–42) dimers by CaM in CGN, up to 120 ± 13 picomoles of Aβ(1–42) /2.5 × 106 cells. Using fluorescence microscopy imaging, we showed an extensive co-localization of CaM and Aβ(1–42) in lipid rafts in CGN stained with up to 100 picomoles of Aβ(1–42)-HiLyteTM-Fluor555 monomers. Intracellular Aβ(1–42) concentration in this range was achieved by 2 h incubation of CGN with 2 μM Aβ(1–42), and this treatment lowered the resting cytosolic calcium of mature CGN in partially depolarizing 25 mM potassium medium. We conclude that the primary cause of the resting cytosolic calcium decrease is the inhibition of L-type calcium channels of CGN by Aβ(1–42) dimers, whose activity is inhibited by CaM:Aβ(1–42) complexes bound to lipid rafts. Full article
(This article belongs to the Special Issue Raft Microdomains and Cell Signaling)
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14 pages, 4527 KiB  
Article
Nitrogen Starvation and Stationary Phase Lipophagy Have Distinct Molecular Mechanisms
by Ravinder Kumar, Muhammad Arifur Rahman and Taras Y. Nazarko
Int. J. Mol. Sci. 2020, 21(23), 9094; https://doi.org/10.3390/ijms21239094 - 29 Nov 2020
Cited by 12 | Viewed by 3947
Abstract
In yeast, the selective autophagy of intracellular lipid droplets (LDs) or lipophagy can be induced by either nitrogen (N) starvation or carbon limitation (e.g., in the stationary (S) phase). We developed the yeast, Komagataella phaffii (formerly Pichia pastoris), as a new lipophagy [...] Read more.
In yeast, the selective autophagy of intracellular lipid droplets (LDs) or lipophagy can be induced by either nitrogen (N) starvation or carbon limitation (e.g., in the stationary (S) phase). We developed the yeast, Komagataella phaffii (formerly Pichia pastoris), as a new lipophagy model and compared the N-starvation and S-phase lipophagy in over 30 autophagy-related mutants using the Erg6-GFP processing assay. Surprisingly, two lipophagy pathways had hardly overlapping stringent molecular requirements. While the N-starvation lipophagy strictly depended on the core autophagic machinery (Atg1-Atg9, Atg18, and Vps15), vacuole fusion machinery (Vam7 and Ypt7), and vacuolar proteolysis (proteinases A and B), only Atg6 and proteinases A and B were essential for the S-phase lipophagy. The rest of the proteins were only partially required in the S-phase. Moreover, we isolated the prl1 (for the positive regulator of lipophagy 1) mutant affected in the S-phase lipophagy, but not N-starvation lipophagy. The prl1 defect was at a stage of delivery of the LDs from the cytoplasm to the vacuole, further supporting the mechanistically different nature of the two lipophagy pathways. Taken together, our results suggest that N-starvation and S-phase lipophagy have distinct molecular mechanisms. Full article
(This article belongs to the Special Issue Raft Microdomains and Cell Signaling)
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Review

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24 pages, 1217 KiB  
Review
Multiplicity of Glycosphingolipid-Enriched Microdomain-Driven Immune Signaling
by Noriko Yokoyama, Kei Hanafusa, Tomomi Hotta, Eriko Oshima, Kazuhisa Iwabuchi and Hitoshi Nakayama
Int. J. Mol. Sci. 2021, 22(17), 9565; https://doi.org/10.3390/ijms22179565 - 03 Sep 2021
Cited by 8 | Viewed by 3297
Abstract
Glycosphingolipids (GSLs), together with cholesterol, sphingomyelin (SM), and glycosylphosphatidylinositol (GPI)-anchored and membrane-associated signal transduction molecules, form GSL-enriched microdomains. These specialized microdomains interact in a cis manner with various immune receptors, affecting immune receptor-mediated signaling. This, in turn, results in the regulation of a [...] Read more.
Glycosphingolipids (GSLs), together with cholesterol, sphingomyelin (SM), and glycosylphosphatidylinositol (GPI)-anchored and membrane-associated signal transduction molecules, form GSL-enriched microdomains. These specialized microdomains interact in a cis manner with various immune receptors, affecting immune receptor-mediated signaling. This, in turn, results in the regulation of a broad range of immunological functions, including phagocytosis, cytokine production, antigen presentation and apoptosis. In addition, GSLs alone can regulate immunological functions by acting as ligands for immune receptors, and exogenous GSLs can alter the organization of microdomains and microdomain-associated signaling. Many pathogens, including viruses, bacteria and fungi, enter host cells by binding to GSL-enriched microdomains. Intracellular pathogens survive inside phagocytes by manipulating intracellular microdomain-driven signaling and/or sphingolipid metabolism pathways. This review describes the mechanisms by which GSL-enriched microdomains regulate immune signaling. Full article
(This article belongs to the Special Issue Raft Microdomains and Cell Signaling)
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17 pages, 3065 KiB  
Review
Lipid Droplets and Their Autophagic Turnover via the Raft-Like Vacuolar Microdomains
by Muhammad Arifur Rahman, Ravinder Kumar, Enrique Sanchez and Taras Y. Nazarko
Int. J. Mol. Sci. 2021, 22(15), 8144; https://doi.org/10.3390/ijms22158144 - 29 Jul 2021
Cited by 11 | Viewed by 6838
Abstract
Although once perceived as inert structures that merely serve for lipid storage, lipid droplets (LDs) have proven to be the dynamic organelles that hold many cellular functions. The LDs’ basic structure of a hydrophobic core consisting of neutral lipids and enclosed in a [...] Read more.
Although once perceived as inert structures that merely serve for lipid storage, lipid droplets (LDs) have proven to be the dynamic organelles that hold many cellular functions. The LDs’ basic structure of a hydrophobic core consisting of neutral lipids and enclosed in a phospholipid monolayer allows for quick lipid accessibility for intracellular energy and membrane production. Whereas formed at the peripheral and perinuclear endoplasmic reticulum, LDs are degraded either in the cytosol by lipolysis or in the vacuoles/lysosomes by autophagy. Autophagy is a regulated breakdown of dysfunctional, damaged, or surplus cellular components. The selective autophagy of LDs is called lipophagy. Here, we review LDs and their degradation by lipophagy in yeast, which proceeds via the micrometer-scale raft-like lipid domains in the vacuolar membrane. These vacuolar microdomains form during nutrient deprivation and facilitate internalization of LDs via the vacuolar membrane invagination and scission. The resultant intra-vacuolar autophagic bodies with LDs inside are broken down by vacuolar lipases and proteases. This type of lipophagy is called microlipophagy as it resembles microautophagy, the type of autophagy when substrates are sequestered right at the surface of a lytic compartment. Yeast microlipophagy via the raft-like vacuolar microdomains is a great model system to study the role of lipid domains in microautophagic pathways. Full article
(This article belongs to the Special Issue Raft Microdomains and Cell Signaling)
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18 pages, 54315 KiB  
Review
Lipid Rafts and Dopamine Receptor Signaling
by Victor J. Martinez, Laureano D. Asico, Pedro A. Jose and Andrew C. Tiu
Int. J. Mol. Sci. 2020, 21(23), 8909; https://doi.org/10.3390/ijms21238909 - 24 Nov 2020
Cited by 15 | Viewed by 3900
Abstract
The renal dopaminergic system has been identified as a modulator of sodium balance and blood pressure. According to the Centers for Disease Control and Prevention, in 2018 in the United States, almost half a million deaths included hypertension as a primary or contributing [...] Read more.
The renal dopaminergic system has been identified as a modulator of sodium balance and blood pressure. According to the Centers for Disease Control and Prevention, in 2018 in the United States, almost half a million deaths included hypertension as a primary or contributing cause. Renal dopamine receptors, members of the G protein-coupled receptor family, are divided in two groups: D1-like receptors that act to keep the blood pressure in the normal range, and D2-like receptors with a variable effect on blood pressure, depending on volume status. The renal dopamine receptor function is regulated, in part, by its expression in microdomains in the plasma membrane. Lipid rafts form platforms within the plasma membrane for the organization and dynamic contact of molecules involved in numerous cellular processes such as ligand binding, membrane sorting, effector specificity, and signal transduction. Understanding all the components of lipid rafts, their interaction with renal dopamine receptors, and their signaling process offers an opportunity to unravel potential treatment targets that could halt the progression of hypertension, chronic kidney disease (CKD), and their complications. Full article
(This article belongs to the Special Issue Raft Microdomains and Cell Signaling)
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