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Molecular Regulation of the Endomembrane System
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Molecular Regulation of the Endomembrane System

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

Deadline for manuscript submissions: closed (17 May 2019) | Viewed by 88136

Special Issue Editor

Prof. Dr. Jeremy Simpson

E-Mail Website
Guest Editor
School of Biology and Environmental Science, Science Centre - West, University College Dublin, Belfield, Dublin 4, Ireland
Interests: organisation and regulation of eukaryotic membrane traffic pathways
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

One striking observation in eukaryotic cells is that over time their organelles maintain a remarkably constant size and shape despite high levels of biochemical activity. In the early secretory pathway, for example, proteins synthesised in the endoplasmic reticulum (ER) but which are destined for secretion are constantly packaged into membrane transport carriers that leave the ER and are directed towards the Golgi complex. The fact that the ER maintains its overall size, shape, and volume tells us that this organelle must receive—from the Golgi complex—an equivalent amount of membrane per unit time. Indeed, if all the organelles in the endomembrane system are to retain their functionality, such counter-balancing of the membrane flow must exist between all compartments that communicate with each other. This control of the endomembrane system is achieved through a variety of factors, including the activity of proteins and lipids resident in each compartment, as well as through long-range signalling events across the cell, and linkage to the cytoskeleton. What is also clear is that perturbation of transport pathways between organelles, manifested in a number of diseases, results in aberrant organelle function and morphology.

In this Special Issue entitled "Molecular Regulation of the Endomembrane System", we are seeking novel research or review articles highlighting the variety of machinery and regulatory mechanisms used in membrane traffic, with specific regard to how membrane flux is controlled and how it determines the identity and function of organelles. Also relevant is how dysfunctional trafficking events have implications in disease. We are open to articles addressing the molecular control of membrane traffic in a variety of model systems. We look forward to receiving your contributions to this exciting Special Issue.

Prof. Dr. Jeremy C. Simpson
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

  • membrane traffic
  • secretory pathway
  • endocytic pathway
  • organelle identity
  • coat proteins
  • small GTPases
  • lipids and phosphoinositides
  • endoplasmic reticulum
  • Golgi complex endosomal system
  • cytoskeleton
  • signalling pathways
  • disease, infection, and membrane traffic

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Published Papers (10 papers)

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Editorial

Jump to: Research, Review

4 pages, 176 KiB  
Editorial
Modification of the Mammalian Endomembrane System in Healthy and Diseased Cells
by Jeremy C. Simpson
Int. J. Mol. Sci. 2020, 21(6), 2133; https://doi.org/10.3390/ijms21062133 - 20 Mar 2020
Cited by 3 | Viewed by 2228
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

Jump to: Editorial, Review

15 pages, 3016 KiB  
Article
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://doi.org/10.3390/ijms20092192 - 3 May 2019
Cited by 15 | Viewed by 3273
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

Jump to: Editorial, Research

15 pages, 1076 KiB  
Review
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://doi.org/10.3390/ijms20163916 - 12 Aug 2019
Cited by 33 | Viewed by 6718
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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Graphical abstract

16 pages, 2360 KiB  
Review
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://doi.org/10.3390/ijms20143506 - 17 Jul 2019
Cited by 26 | Viewed by 9331
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  
Review
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://doi.org/10.3390/ijms20102586 - 27 May 2019
Cited by 25 | Viewed by 6021
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  
Review
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://doi.org/10.3390/ijms20092336 - 11 May 2019
Cited by 26 | Viewed by 5700
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  
Review
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://doi.org/10.3390/ijms20092167 - 1 May 2019
Cited by 490 | Viewed by 28680
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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Graphical abstract

10 pages, 1036 KiB  
Review
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://doi.org/10.3390/ijms20082028 - 24 Apr 2019
Cited by 21 | Viewed by 4970
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  
Review
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://doi.org/10.3390/ijms20081996 - 23 Apr 2019
Cited by 47 | Viewed by 12053
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  
Review
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://doi.org/10.3390/ijms20071792 - 11 Apr 2019
Cited by 32 | Viewed by 8063
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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