Editorial

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4 pages, 176 KiB

Open AccessEditorial

Modification of the Mammalian Endomembrane System in Healthy and Diseased Cells

by Jeremy C. Simpson

Int. J. Mol. Sci. 2020, 21(6), 2133; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21062133 - 20 Mar 2020

Cited by 3 | Viewed by 1880

Abstract

One remarkable characteristic of eukaryotic cells is the complexity of their membrane systems [...] Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

Research

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15 pages, 3016 KiB

Open AccessArticle

Zinc Attenuates the Cytotoxicity of Some Stimuli by Reducing Endoplasmic Reticulum Stress in Hepatocytes

by Masashi Kusanaga, Shinji Oe, Noriyoshi Ogino, Sota Minami, Koichiro Miyagawa, Yuichi Honma and Masaru Harada

Int. J. Mol. Sci. 2019, 20(9), 2192; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20092192 - 03 May 2019

Cited by 13 | Viewed by 2870

Abstract

Zinc is an essential trace element and plays critical roles in cellular integrity and biological functions. Excess copper induced both oxidative stress and endoplasmic reticulum (ER) stress in liver-derived cultured cells. Excess copper also induced impairment of autophagic flux at the step of [...] Read more.

Zinc is an essential trace element and plays critical roles in cellular integrity and biological functions. Excess copper induced both oxidative stress and endoplasmic reticulum (ER) stress in liver-derived cultured cells. Excess copper also induced impairment of autophagic flux at the step of autophagosome–lysosome fusion, as well as Mallory–Denk body (MDB)-like inclusion body formation. Zinc ameliorated excess copper-induced impairment of autophagic flux and MDB-like inclusion body formation via the maintenance of ER homeostasis. Furthermore, zinc also ameliorated free fatty acid-induced impairment of autophagic flux. These results indicate that zinc may be able to protect hepatocytes from various ER stress-related conditions. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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Review

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15 pages, 1076 KiB

Open AccessReview

Multitasking Rab Proteins in Autophagy and Membrane Trafficking: A Focus on Rab33b

by Niamh E. Morgan, Meritxell B. Cutrona and Jeremy C. Simpson

Int. J. Mol. Sci. 2019, 20(16), 3916; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20163916 - 12 Aug 2019

Cited by 30 | Viewed by 5949

Abstract

Autophagy (particularly macroautophagy) is a bulk degradation process used by eukaryotic cells in order to maintain adequate energy levels and cellular homeostasis through the delivery of long-lived proteins and organelles to the lysosome, resulting in their degradation. It is becoming increasingly clear that [...] Read more.

Autophagy (particularly macroautophagy) is a bulk degradation process used by eukaryotic cells in order to maintain adequate energy levels and cellular homeostasis through the delivery of long-lived proteins and organelles to the lysosome, resulting in their degradation. It is becoming increasingly clear that many of the molecular requirements to fulfil autophagy intersect with those of conventional and unconventional membrane trafficking pathways. Of particular interest is the dependence of these processes on multiple members of the Rab family of small GTP binding proteins. Rab33b is a protein that localises to the Golgi apparatus and has suggested functions in both membrane trafficking and autophagic processes. Interestingly, mutations in the RAB33B gene have been reported to cause the severe skeletal disorder, Smith–McCort Dysplasia; however, the molecular basis for Rab33b in this disorder remains to be determined. In this review, we focus on the current knowledge of the participation of Rab33b and its interacting partners in membrane trafficking and macroautophagy, and speculate on how its function, and dysfunction, may contribute to human disease. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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16 pages, 2360 KiB

Open AccessReview

Endoplasmic Reticulum Export of GPI-Anchored Proteins

by Sergio Lopez, Sofia Rodriguez-Gallardo, Susana Sabido-Bozo and Manuel Muñiz

Int. J. Mol. Sci. 2019, 20(14), 3506; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20143506 - 17 Jul 2019

Cited by 25 | Viewed by 8578

Abstract

Protein export from the endoplasmic reticulum (ER) is an essential process in all eukaryotes driven by the cytosolic coat complex COPII, which forms vesicles at ER exit sites for transport of correctly assembled secretory cargo to the Golgi apparatus. The COPII machinery must [...] Read more.

Protein export from the endoplasmic reticulum (ER) is an essential process in all eukaryotes driven by the cytosolic coat complex COPII, which forms vesicles at ER exit sites for transport of correctly assembled secretory cargo to the Golgi apparatus. The COPII machinery must adapt to the existing wide variety of different types of cargo proteins and to different cellular needs for cargo secretion. The study of the ER export of glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs), a special glycolipid-linked class of cell surface proteins, is contributing to address these key issues. Due to their special biophysical properties, GPI-APs use a specialized COPII machinery to be exported from the ER and their processing and maturation has been recently shown to actively regulate COPII function. In this review, we discuss the regulatory mechanisms by which GPI-APs are assembled and selectively exported from the ER. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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27 pages, 814 KiB

Open AccessReview

The Biology of the Nuclear Envelope and Its Implications in Cancer Biology

by Maria Alvarado-Kristensson and Catalina Ana Rosselló

Int. J. Mol. Sci. 2019, 20(10), 2586; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20102586 - 27 May 2019

Cited by 24 | Viewed by 5315

Abstract

The formation of the nuclear envelope and the subsequent compartmentalization of the genome is a defining feature of eukaryotes. Traditionally, the nuclear envelope was purely viewed as a physical barrier to preserve genetic material in eukaryotic cells. However, in the last few decades, [...] Read more.

The formation of the nuclear envelope and the subsequent compartmentalization of the genome is a defining feature of eukaryotes. Traditionally, the nuclear envelope was purely viewed as a physical barrier to preserve genetic material in eukaryotic cells. However, in the last few decades, it has been revealed to be a critical cellular component in controlling gene expression and has been implicated in several human diseases. In cancer, the relevance of the cell nucleus was first reported in the mid-1800s when an altered nuclear morphology was observed in tumor cells. This review aims to give a current and comprehensive view of the role of the nuclear envelope on cancer first by recapitulating the changes of the nuclear envelope during cell division, second, by reviewing the role of the nuclear envelope in cell cycle regulation, signaling, and the regulation of the genome, and finally, by addressing the nuclear envelope link to cell migration and metastasis and its use in cancer prognosis. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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13 pages, 1288 KiB

Open AccessReview

Flavivirus Replication Organelle Biogenesis in the Endoplasmic Reticulum: Comparison with Other Single-Stranded Positive-Sense RNA Viruses

by Masashi Arakawa and Eiji Morita

Int. J. Mol. Sci. 2019, 20(9), 2336; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20092336 - 11 May 2019

Cited by 24 | Viewed by 5042

Abstract

Some single-stranded positive-sense RNA [ssRNA(+)] viruses, including Flavivirus, generate specific organelle-like structures in the host endoplasmic reticulum (ER). These structures are called virus replication organelles and consist of two distinct subdomains, the vesicle packets (VPs) and the convoluted membranes (CMs). The VPs are [...] Read more.

Some single-stranded positive-sense RNA [ssRNA(+)] viruses, including Flavivirus, generate specific organelle-like structures in the host endoplasmic reticulum (ER). These structures are called virus replication organelles and consist of two distinct subdomains, the vesicle packets (VPs) and the convoluted membranes (CMs). The VPs are clusters of small vesicle compartments and are considered to be the site of viral genome replication. The CMs are electron-dense amorphous structures observed in proximity to the VPs, but the exact roles of CMs are mostly unknown. Several recent studies have revealed that flaviviruses recruit several host factors that are usually used for the biogenesis of other conventional organelles and usurp their function to generate virus replication organelles. In the current review, we summarize recent studies focusing on the role of host factors in the formation of virus replication organelles and discuss how these intricate membrane structures are organized. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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30 pages, 2514 KiB

Open AccessReview

Membrane Lipid Composition: Effect on Membrane and Organelle Structure, Function and Compartmentalization and Therapeutic Avenues

by Doralicia Casares, Pablo V. Escribá and Catalina Ana Rosselló

Int. J. Mol. Sci. 2019, 20(9), 2167; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20092167 - 01 May 2019

Cited by 422 | Viewed by 24671

Abstract

Biological membranes are key elements for the maintenance of cell architecture and physiology. Beyond a pure barrier separating the inner space of the cell from the outer, the plasma membrane is a scaffold and player in cell-to-cell communication and the initiation of intracellular [...] Read more.

Biological membranes are key elements for the maintenance of cell architecture and physiology. Beyond a pure barrier separating the inner space of the cell from the outer, the plasma membrane is a scaffold and player in cell-to-cell communication and the initiation of intracellular signals among other functions. Critical to this function is the plasma membrane compartmentalization in lipid microdomains that control the localization and productive interactions of proteins involved in cell signal propagation. In addition, cells are divided into compartments limited by other membranes whose integrity and homeostasis are finely controlled, and which determine the identity and function of the different organelles. Here, we review current knowledge on membrane lipid composition in the plasma membrane and endomembrane compartments, emphasizing its role in sustaining organelle structure and function. The correct composition and structure of cell membranes define key pathophysiological aspects of cells. Therefore, we explore the therapeutic potential of manipulating membrane lipid composition with approaches like membrane lipid therapy, aiming to normalize cell functions through the modification of membrane lipid bilayers. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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10 pages, 1036 KiB

Open AccessReview

Acyl-CoA-Binding Domain-Containing 3 (ACBD3; PAP7; GCP60): A Multi-Functional Membrane Domain Organizer

by Xihua Yue, Yi Qian, Bopil Gim and Intaek Lee

Int. J. Mol. Sci. 2019, 20(8), 2028; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20082028 - 24 Apr 2019

Cited by 19 | Viewed by 4416

Abstract

Acyl-CoA-binding domain-containing 3 (ACBD3) is a multi-functional scaffolding protein, which has been associated with a diverse array of cellular functions, including steroidogenesis, embryogenesis, neurogenesis, Huntington’s disease (HD), membrane trafficking, and viral/bacterial proliferation in infected host cells. In this review, we aim to give [...] Read more.

Acyl-CoA-binding domain-containing 3 (ACBD3) is a multi-functional scaffolding protein, which has been associated with a diverse array of cellular functions, including steroidogenesis, embryogenesis, neurogenesis, Huntington’s disease (HD), membrane trafficking, and viral/bacterial proliferation in infected host cells. In this review, we aim to give a timely overview of recent findings on this protein, including its emerging role in membrane domain organization at the Golgi and the mitochondria. We hope that this review provides readers with useful insights on how ACBD3 may contribute to membrane domain organization along the secretory pathway and on the cytoplasmic surface of intracellular organelles, which influence many important physiological and pathophysiological processes in mammalian cells. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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40 pages, 6942 KiB

Open AccessReview

Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition

by Katharine A. Michie, Adam Bermeister, Neil O. Robertson, Sophia C. Goodchild and Paul M. G. Curmi

Int. J. Mol. Sci. 2019, 20(8), 1996; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20081996 - 23 Apr 2019

Cited by 44 | Viewed by 10905

Abstract

The merlin-ERM (ezrin, radixin, moesin) family of proteins plays a central role in linking the cellular membranes to the cortical actin cytoskeleton. Merlin regulates contact inhibition and is an integral part of cell–cell junctions, while ERM proteins, ezrin, radixin and moesin, assist in [...] Read more.

The merlin-ERM (ezrin, radixin, moesin) family of proteins plays a central role in linking the cellular membranes to the cortical actin cytoskeleton. Merlin regulates contact inhibition and is an integral part of cell–cell junctions, while ERM proteins, ezrin, radixin and moesin, assist in the formation and maintenance of specialized plasma membrane structures and membrane vesicle structures. These two protein families share a common evolutionary history, having arisen and separated via gene duplication near the origin of metazoa. During approximately 0.5 billion years of evolution, the merlin and ERM family proteins have maintained both sequence and structural conservation to an extraordinary level. Comparing crystal structures of merlin-ERM proteins and their complexes, a picture emerges of the merlin-ERM proteins acting as switchable interaction hubs, assembling protein complexes on cellular membranes and linking them to the actin cytoskeleton. Given the high level of structural conservation between the merlin and ERM family proteins we speculate that they may function together. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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25 pages, 1872 KiB

Open AccessReview

Stressed: The Unfolded Protein Response in T Cell Development, Activation, and Function

by Kyeorda Kemp and Cody Poe

Int. J. Mol. Sci. 2019, 20(7), 1792; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20071792 - 11 Apr 2019

Cited by 27 | Viewed by 7361

Abstract

The unfolded protein response (UPR) is a highly conserved pathway that allows cells to respond to stress in the endoplasmic reticulum caused by an accumulation of misfolded and unfolded protein. This is of great importance to secretory cells because, in order for proteins [...] Read more.

The unfolded protein response (UPR) is a highly conserved pathway that allows cells to respond to stress in the endoplasmic reticulum caused by an accumulation of misfolded and unfolded protein. This is of great importance to secretory cells because, in order for proteins to traffic from the endoplasmic reticulum (ER), they need to be folded appropriately. While a wealth of literature has implicated UPR in immune responses, less attention has been given to the role of UPR in T cell development and function. This review discusses the importance of UPR in T cell development, homeostasis, activation, and effector functions. We also speculate about how UPR may be manipulated in T cells to ameliorate pathologies. Full article

(This article belongs to the Special Issue Molecular Regulation of the Endomembrane System)

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