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Special Issue "Regulation of Membrane Trafficking and Its Potential Implications"

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

Deadline for manuscript submissions: closed (31 March 2013)

Special Issue Editor

Guest Editor
Prof. Dr. Jeremy C. Simpson (Website)

University College Dublin, School of Biology and Environmental Science, Science Center - West, Belfield, Dublin 4, Ireland
Phone: +353 1 716 2345
Interests: organisation and regulation of eukaryotic membrane traffic pathways

Special Issue Information

Dear Colleagues,

Membrane trafficking pathways play a vital role in cells, providing critical communication links throughout the endomembrane system, ensuring that protein and lipid cargo are distributed in a timely manner. Following the pioneering work of Porter, Claude and Palade, the recent decades have witnessed a truly extensive array of techniques being applied to the study of membrane traffic, revealing an enormous variety and complexity of regulatory machinery. Furthermore, it is becoming increasingly clear that membrane traffic is also highly interconnected with other cellular processes allowing cells to respond to stimuli and insult in remarkable and dynamic ways. In this special issue entitled "Regulation of Membrane Trafficking and Its Potential Implications", we are seeking novel research or review articles highlighting the variety of machinery and regulatory mechanisms used in membrane traffic, the importance of how membrane traffic is interlinked to other cellular events and processes, and also how dysfunctional trafficking machinery has implications in disease and infection. We look forward to receiving your contributions to this exciting special issue.

Prof. Dr. Jeremy C. Simpson
Guest Editor

Submission

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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a 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 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 1600 CHF.

Keywords

  • membrane traffic
  • secretory pathway
  • endocytosis and internalisation pathways
  • coat proteins
  • small GTPases
  • lipids, phosphoinositides and membrane traffic
  • cytoskeleton and membrane traffic
  • signalling pathways and membrane traffic
  • disease, infection and membrane traffic

Related Special Issue

Published Papers (17 papers)

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Research

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Open AccessArticle Characterization of a Gene Encoding Clathrin Heavy Chain in Maize Up-Regulated by Salicylic Acid, Abscisic Acid and High Boron Supply
Int. J. Mol. Sci. 2013, 14(7), 15179-15198; doi:10.3390/ijms140715179
Received: 16 May 2013 / Revised: 1 July 2013 / Accepted: 16 July 2013 / Published: 22 July 2013
Cited by 5 | PDF Full-text (2645 KB) | HTML Full-text | XML Full-text
Abstract
Clathrin, a three-legged triskelion composed of three clathrin heavy chains (CHCs) and three light chains (CLCs), plays a critical role in clathrin-mediated endocytosis (CME) in eukaryotic cells. In this study, the genes ZmCHC1 and ZmCHC2 encoding clathrin heavy chain in maize were [...] Read more.
Clathrin, a three-legged triskelion composed of three clathrin heavy chains (CHCs) and three light chains (CLCs), plays a critical role in clathrin-mediated endocytosis (CME) in eukaryotic cells. In this study, the genes ZmCHC1 and ZmCHC2 encoding clathrin heavy chain in maize were cloned and characterized for the first time in monocots. ZmCHC1 encodes a 1693-amino acid-protein including 29 exons and 28 introns, and ZmCHC2 encodes a 1746-amino acid-protein including 28 exons and 27 introns. The high similarities of gene structure, protein sequences and 3D models among ZmCHC1, and Arabidopsis AtCHC1 and AtCHC2 suggest their similar functions in CME. ZmCHC1 gene is predominantly expressed in maize roots instead of ubiquitous expression of ZmCHC2. Consistent with a typical predicted salicylic acid (SA)-responsive element and four predicted ABA-responsive elements (ABREs) in the promoter sequence of ZmCHC1, the expression of ZmCHC1 instead of ZmCHC2 in maize roots is significantly up-regulated by SA or ABA, suggesting that ZmCHC1 gene may be involved in the SA signaling pathway in maize defense responses. The expressions of ZmCHC1 and ZmCHC2 genes in maize are down-regulated by azide or cold treatment, further revealing the energy requirement of CME and suggesting that CME in plants is sensitive to low temperatures. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessArticle Sequestration of AS-DACA into Acidic Compartments of the Membrane Trafficking System as a Mechanism of Drug Resistance in Rhabdomyosarcoma
Int. J. Mol. Sci. 2013, 14(7), 13042-13062; doi:10.3390/ijms140713042
Received: 16 April 2013 / Revised: 30 May 2013 / Accepted: 5 June 2013 / Published: 25 June 2013
Cited by 1 | PDF Full-text (2095 KB) | HTML Full-text | XML Full-text
Abstract
The accumulation of weakly basic drugs into acidic organelles has recently been described as a contributor to resistance in childhood cancer rhabdomyosarcoma (RMS) cell lines with differential sensitivity to a novel topoisomerase II inhibitor, AS-DACA. The current study aims to explore the [...] Read more.
The accumulation of weakly basic drugs into acidic organelles has recently been described as a contributor to resistance in childhood cancer rhabdomyosarcoma (RMS) cell lines with differential sensitivity to a novel topoisomerase II inhibitor, AS-DACA. The current study aims to explore the contribution of the endocytic pathway to AS-DACA sequestration in RMS cell lines. A 24-fold differential in AS-DACA cytotoxicity was detected between the RMS lines RD and Rh30. The effect of inhibitors of the endocytic pathway on AS-DACA sensitivity in RMS cell lines, coupled with the variations of endosomal marker expression, indicated the late endosomal/lysosomal compartment was implicated by confounding lines of evidence. Higher expression levels of Lysosomal-Associated Membrane Protein-1 (LAMP1) in the resistant RMS cell line, RD, provided correlations between the increased amount and activity of these compartments to AS-DACA resistance. The late endosomal inhibitor 3-methyladenine increased AS-DACA sensitivity solely in RD leading to the reduction of AS-DACA in membrane trafficking organelles. Acidification inhibitors did not produce an increase in AS-DACA sensitivity nor reduce its sequestration, indicating that the pH partitioning of weakly basic drugs into acidic compartments does not likely contribute to the AS-DACA sequestering resistance mechanism evident in RMS cells. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessArticle Loss of Vps54 Function Leads to Vesicle Traffic Impairment, Protein Mis-Sorting and Embryonic Lethality
Int. J. Mol. Sci. 2013, 14(6), 10908-10925; doi:10.3390/ijms140610908
Received: 3 April 2013 / Revised: 30 April 2013 / Accepted: 3 May 2013 / Published: 24 May 2013
Cited by 10 | PDF Full-text (1739 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The identification of the mutation causing the phenotype of the amyotrophic lateral sclerosis (ALS) model mouse, wobbler, has linked motor neuron degeneration with retrograde vesicle traffic. The wobbler mutation affects protein stability of Vps54, a ubiquitously expressed vesicle-tethering factor and leads to [...] Read more.
The identification of the mutation causing the phenotype of the amyotrophic lateral sclerosis (ALS) model mouse, wobbler, has linked motor neuron degeneration with retrograde vesicle traffic. The wobbler mutation affects protein stability of Vps54, a ubiquitously expressed vesicle-tethering factor and leads to partial loss of Vps54 function. Moreover, the Vps54 null mutation causes embryonic lethality, which is associated with extensive membrane blebbing in the neural tube and is most likely a consequence of impaired vesicle transport. Investigation of cells derived from wobbler and Vps54 null mutant embryos demonstrates impaired retrograde transport of the Cholera-toxin B subunit to the trans-Golgi network and mis-sorting of mannose-6-phosphate receptors and cargo proteins dependent on retrograde vesicle transport. Endocytosis assays demonstrate no difference between wobbler and wild type cells, indicating that the retrograde vesicle traffic to the trans-Golgi network, but not endocytosis, is affected in Vps54 mutant cells. The results obtained on wobbler cells were extended to test the use of cultured skin fibroblasts from human ALS patients to investigate the retrograde vesicle traffic. Analysis of skin fibroblasts of ALS patients will support the investigation of the critical role of the retrograde vesicle transport in ALS pathogenesis and might yield a diagnostic prospect. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessArticle The Influence of Polyunsaturated Fatty Acids on the Phospholipase D Isoforms Trafficking and Activity in Mast Cells
Int. J. Mol. Sci. 2013, 14(5), 9005-9017; doi:10.3390/ijms14059005
Received: 26 March 2013 / Revised: 15 April 2013 / Accepted: 18 April 2013 / Published: 25 April 2013
Cited by 2 | PDF Full-text (1099 KB) | HTML Full-text | XML Full-text
Abstract
The impact of polyunsaturated fatty acid (PUFA) supplementation on phospholipase D (PLD) trafficking and activity in mast cells was investigated. The enrichment of mast cells with different PUFA including α-linolenic acid (LNA), eicosapentaenoic acid (EPA), docosahexaenoic acid (DHA), linoleic acid (LA) or [...] Read more.
The impact of polyunsaturated fatty acid (PUFA) supplementation on phospholipase D (PLD) trafficking and activity in mast cells was investigated. The enrichment of mast cells with different PUFA including α-linolenic acid (LNA), eicosapentaenoic acid (EPA), docosahexaenoic acid (DHA), linoleic acid (LA) or arachidonic acid (AA) revealed a PUFA-mediated modulation of the mastoparan-stimulated PLD trafficking and activity. All PUFA examined, except AA, prevented the migration of the PLD1 to the plasma membrane. For PLD2 no PUFA effects on trafficking could be observed. Moreover, PUFA supplementation resulted in an increase of mastoparan-stimulated total PLD activity, which correlated with the number of double bonds of the supplemented fatty acids. To investigate, which PLD isoform was affected by PUFA, stimulated mast cells were supplemented with DHA or AA in the presence of specific PLD-isoform inhibitors. It was found that both DHA and AA diminished the inhibition of PLD activity in the presence of a PLD1 inhibitor. By contrast, only AA diminished the inhibition of PLD activity in the presence of a PLD2 inhibitor. Thus, PUFA modulate the trafficking and activity of PLD isoforms in mast cells differently. This may, in part, account for the immunomodulatory effect of unsaturated fatty acids and contributes to our understanding of the modulation of mast cell activity by PUFA. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)

Review

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Open AccessReview Human Diseases Associated with Form and Function of the Golgi Complex
Int. J. Mol. Sci. 2013, 14(9), 18670-18681; doi:10.3390/ijms140918670
Received: 23 July 2013 / Revised: 9 August 2013 / Accepted: 3 September 2013 / Published: 10 September 2013
Cited by 8 | PDF Full-text (1221 KB) | HTML Full-text | XML Full-text
Abstract
The Golgi complex lies at the heart of the secretory pathway and is responsible for modifying proteins and lipids, as well as sorting newly synthesized molecules to their correct destination. As a consequence of these important roles, any changes in its proteome [...] Read more.
The Golgi complex lies at the heart of the secretory pathway and is responsible for modifying proteins and lipids, as well as sorting newly synthesized molecules to their correct destination. As a consequence of these important roles, any changes in its proteome can negatively affect its function and in turn lead to disease. Recently, a number of proteins have been identified, which when either depleted or mutated, result in diseases that affect various organ systems. Here we describe how these proteins have been linked to the Golgi complex, and specifically how they affect either the morphology, membrane traffic or glycosylation ability of this organelle. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview ARF1 and SAR1 GTPases in Endomembrane Trafficking in Plants
Int. J. Mol. Sci. 2013, 14(9), 18181-18199; doi:10.3390/ijms140918181
Received: 30 March 2013 / Revised: 19 August 2013 / Accepted: 20 August 2013 / Published: 5 September 2013
Cited by 3 | PDF Full-text (359 KB) | HTML Full-text | XML Full-text
Abstract
Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their [...] Read more.
Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics. The ARF1 and SAR1 GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. ARF1 has been shown to play a critical role in COPI (Coat Protein Complex I)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular COPII-mediated protein trafficking from the ER to the Golgi apparatus. This review offers a summary of vesicular trafficking with an emphasis on the ARF1 and SAR1 expression patterns at early growth stages and in the de-etiolation process. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview Membrane Trafficking of Death Receptors: Implications on Signalling
Int. J. Mol. Sci. 2013, 14(7), 14475-14503; doi:10.3390/ijms140714475
Received: 9 May 2013 / Revised: 19 June 2013 / Accepted: 27 June 2013 / Published: 11 July 2013
Cited by 13 | PDF Full-text (3686 KB) | HTML Full-text | XML Full-text
Abstract
Death receptors were initially recognised as potent inducers of apoptotic cell death and soon ambitious attempts were made to exploit selective ignition of controlled cellular suicide as therapeutic strategy in malignant diseases. However, the complexity of death receptor signalling has increased substantially [...] Read more.
Death receptors were initially recognised as potent inducers of apoptotic cell death and soon ambitious attempts were made to exploit selective ignition of controlled cellular suicide as therapeutic strategy in malignant diseases. However, the complexity of death receptor signalling has increased substantially during recent years. Beyond activation of the apoptotic cascade, involvement in a variety of cellular processes including inflammation, proliferation and immune response was recognised. Mechanistically, these findings raised the question how multipurpose receptors can ensure selective activation of a particular pathway. A growing body of evidence points to an elegant spatiotemporal regulation of composition and assembly of the receptor-associated signalling complex. Upon ligand binding, receptor recruitment in specialized membrane compartments, formation of receptor-ligand clusters and internalisation processes constitute key regulatory elements. In this review, we will summarise the current concepts of death receptor trafficking and its implications on receptor-associated signalling events. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview Astrocytic Vesicle Mobility in Health and Disease
Int. J. Mol. Sci. 2013, 14(6), 11238-11258; doi:10.3390/ijms140611238
Received: 1 April 2013 / Revised: 26 April 2013 / Accepted: 8 May 2013 / Published: 27 May 2013
Cited by 14 | PDF Full-text (776 KB) | HTML Full-text | XML Full-text
Abstract
Astrocytes are no longer considered subservient to neurons, and are, instead, now understood to play an active role in brain signaling. The intercellular communication of astrocytes with neurons and other non-neuronal cells involves the exchange of molecules by exocytotic and endocytotic processes [...] Read more.
Astrocytes are no longer considered subservient to neurons, and are, instead, now understood to play an active role in brain signaling. The intercellular communication of astrocytes with neurons and other non-neuronal cells involves the exchange of molecules by exocytotic and endocytotic processes through the trafficking of intracellular vesicles. Recent studies of single vesicle mobility in astrocytes have prompted new views of how astrocytes contribute to information processing in nervous tissue. Here, we review the trafficking of several types of membrane-bound vesicles that are specifically involved in the processes of (i) intercellular communication by gliotransmitters (glutamate, adenosine 5'-triphosphate, atrial natriuretic peptide), (ii) plasma membrane exchange of transporters and receptors (EAAT2, MHC-II), and (iii) the involvement of vesicle mobility carrying aquaporins (AQP4) in water homeostasis. The properties of vesicle traffic in astrocytes are discussed in respect to networking with neighboring cells in physiologic and pathologic conditions, such as amyotrophic lateral sclerosis, multiple sclerosis, and states in which astrocytes contribute to neuroinflammatory conditions. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview New Advances in Urea Transporter UT-A1 Membrane Trafficking
Int. J. Mol. Sci. 2013, 14(5), 10674-10682; doi:10.3390/ijms140510674
Received: 22 April 2013 / Revised: 9 May 2013 / Accepted: 9 May 2013 / Published: 21 May 2013
Cited by 3 | PDF Full-text (632 KB) | HTML Full-text | XML Full-text
Abstract
The vasopressin-regulated urea transporter UT-A1, expressed in kidney inner medullary collecting duct (IMCD) epithelial cells, plays a critical role in the urinary concentrating mechanisms. As a membrane protein, the function of UT-A1 transport activity relies on its presence in the plasma membrane. [...] Read more.
The vasopressin-regulated urea transporter UT-A1, expressed in kidney inner medullary collecting duct (IMCD) epithelial cells, plays a critical role in the urinary concentrating mechanisms. As a membrane protein, the function of UT-A1 transport activity relies on its presence in the plasma membrane. Therefore, UT-A1 successfully trafficking to the apical membrane of the polarized epithelial cells is crucial for the regulation of urea transport. This review summarizes the research progress of UT-A1 regulation over the past few years, specifically on the regulation of UT-A1 membrane trafficking by lipid rafts, N-linked glycosylation and a group of accessory proteins. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview Rab27 GTPases Distribute Extracellular Nanomaps for Invasive Growth and Metastasis: Implications for Prognosis and Treatment
Int. J. Mol. Sci. 2013, 14(5), 9883-9892; doi:10.3390/ijms14059883
Received: 13 April 2013 / Revised: 19 April 2013 / Accepted: 3 May 2013 / Published: 10 May 2013
Cited by 4 | PDF Full-text (260 KB) | HTML Full-text | XML Full-text
Abstract
The Rab27 family of small GTPases regulates exocytosis of distinct vesicle types including multivesicular endosomes, which results in the release of exosomes. Exosomes are nanometer-sized membrane vesicles that enclose soluble factors such as proteins and nucleic acids within a lipid bilayer and [...] Read more.
The Rab27 family of small GTPases regulates exocytosis of distinct vesicle types including multivesicular endosomes, which results in the release of exosomes. Exosomes are nanometer-sized membrane vesicles that enclose soluble factors such as proteins and nucleic acids within a lipid bilayer and can travel toward distant tissues to influence multiple aspects of cell behavior. In our view that tumors are endocrine organs producing exosomes, Rab27 GTPases and their effector proteins are critical determinants for invasive growth and metastasis. Rab27 proteins and their effectors may serve as prognostic biomarkers or as targets for patient-tailored therapy. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview Posttranslational Modifications of GLUT4 Affect Its Subcellular Localization and Translocation
Int. J. Mol. Sci. 2013, 14(5), 9963-9978; doi:10.3390/ijms14059963
Received: 15 April 2013 / Revised: 2 May 2013 / Accepted: 2 May 2013 / Published: 10 May 2013
Cited by 4 | PDF Full-text (239 KB) | HTML Full-text | XML Full-text
Abstract
The facilitative glucose transporter type 4 (GLUT4) is expressed in adipose and muscle and plays a vital role in whole body glucose homeostasis. In the absence of insulin, only ~1% of cellular GLUT4 is present at the plasma membrane, with the vast [...] Read more.
The facilitative glucose transporter type 4 (GLUT4) is expressed in adipose and muscle and plays a vital role in whole body glucose homeostasis. In the absence of insulin, only ~1% of cellular GLUT4 is present at the plasma membrane, with the vast majority localizing to intracellular organelles. GLUT4 is retained intracellularly by continuous trafficking through two inter-related cycles. GLUT4 passes through recycling endosomes, the trans Golgi network and an insulin-sensitive intracellular compartment, termed GLUT4-storage vesicles or GSVs. It is from GSVs that GLUT4 is mobilized to the cell surface in response to insulin, where it increases the rate of glucose uptake into the cell. As with many physiological responses to external stimuli, this regulated trafficking event involves multiple posttranslational modifications. This review outlines the roles of posttranslational modifications of GLUT4 on its function and insulin-regulated trafficking. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview Molecular Motors and Apical CFTR Traffic in Epithelia
Int. J. Mol. Sci. 2013, 14(5), 9628-9642; doi:10.3390/ijms14059628
Received: 7 April 2013 / Revised: 19 April 2013 / Accepted: 2 May 2013 / Published: 3 May 2013
Cited by 2 | PDF Full-text (561 KB) | HTML Full-text | XML Full-text
Abstract
Intracellular protein traffic plays an important role in the regulation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) chloride channels. Microtubule and actin-based motor proteins direct CFTR movement along trafficking pathways. As shown for other regulatory proteins such as adaptors, the involvement of [...] Read more.
Intracellular protein traffic plays an important role in the regulation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) chloride channels. Microtubule and actin-based motor proteins direct CFTR movement along trafficking pathways. As shown for other regulatory proteins such as adaptors, the involvement of protein motors in CFTR traffic is cell-type specific. Understanding motor specificity provides insight into the biology of the channel and opens opportunity for discovery of organ-specific drug targets for treating CFTR-mediated diseases. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview Where Do They Come from and Where Do They Go: Candidates for Regulating Extracellular Vesicle Formation in Fungi
Int. J. Mol. Sci. 2013, 14(5), 9581-9603; doi:10.3390/ijms14059581
Received: 29 March 2013 / Revised: 11 April 2013 / Accepted: 17 April 2013 / Published: 2 May 2013
Cited by 13 | PDF Full-text (503 KB) | HTML Full-text | XML Full-text
Abstract
In the past few years, extracellular vesicles (EVs) from at least eight fungal species were characterized. EV proteome in four fungal species indicated putative biogenesis pathways and suggested interesting similarities with mammalian exosomes. Moreover, as observed for mammalian exosomes, fungal EVs were [...] Read more.
In the past few years, extracellular vesicles (EVs) from at least eight fungal species were characterized. EV proteome in four fungal species indicated putative biogenesis pathways and suggested interesting similarities with mammalian exosomes. Moreover, as observed for mammalian exosomes, fungal EVs were demonstrated to be immunologically active. Here we review the seminal and most recent findings related to the production of EVs by fungi. Based on the current literature about secretion of fungal molecules and biogenesis of EVs in eukaryotes, we focus our discussion on a list of cellular proteins with the potential to regulate vesicle biogenesis in the fungi. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview Recent Advances in Understanding the Control of Secretory Proteins by the Unfolded Protein Response in Plants
Int. J. Mol. Sci. 2013, 14(5), 9396-9407; doi:10.3390/ijms14059396
Received: 1 April 2013 / Revised: 17 April 2013 / Accepted: 18 April 2013 / Published: 29 April 2013
Cited by 3 | PDF Full-text (1642 KB) | HTML Full-text | XML Full-text
Abstract
The membrane transport system is built on the proper functioning of the endoplasmic reticulum (ER). The accumulation of unfolded proteins in the ER lumen (ER stress) disrupts ER homeostasis and disturbs the transport system. In response to ER stress, eukaryotic cells activate [...] Read more.
The membrane transport system is built on the proper functioning of the endoplasmic reticulum (ER). The accumulation of unfolded proteins in the ER lumen (ER stress) disrupts ER homeostasis and disturbs the transport system. In response to ER stress, eukaryotic cells activate intracellular signaling (named the unfolded protein response, UPR), which contributes to the quality control of secretory proteins. On the other hand, the deleterious effects of UPR on plant health and growth characteristics have frequently been overlooked, due to limited information on this mechanism. However, recent studies have shed light on the molecular mechanism of plant UPR, and a number of its unique characteristics have been elucidated. This study briefly reviews the progress of understanding what is happening in plants under ER stress conditions. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Figures

Open AccessReview Structural Basis of Membrane Trafficking by Rab Family Small G Protein
Int. J. Mol. Sci. 2013, 14(5), 8912-8923; doi:10.3390/ijms14058912
Received: 1 March 2013 / Revised: 1 April 2013 / Accepted: 10 April 2013 / Published: 25 April 2013
Cited by 8 | PDF Full-text (712 KB) | HTML Full-text | XML Full-text
Abstract
The Ras-superfamily of small G proteins is a family of GTP hydrolases that is regulated by GTP/GDP binding states. One member of the Ras-superfamily, Rab, is involved in the regulation of vesicle trafficking, which is critical to endocytosis, biosynthesis, secretion, cell differentiation [...] Read more.
The Ras-superfamily of small G proteins is a family of GTP hydrolases that is regulated by GTP/GDP binding states. One member of the Ras-superfamily, Rab, is involved in the regulation of vesicle trafficking, which is critical to endocytosis, biosynthesis, secretion, cell differentiation and cell growth. The active form of the Rab proteins, which contains GTP, can recruit specific binding partners, such as sorting adaptors, tethering factors, kinases, phosphatases and motor proteins, thereby influencing vesicle formation, transport, and tethering. Many Rab proteins share the same interacting partners and perform unique roles in specific locations. Because functional loss of the Rab pathways has been implicated in a variety of diseases, the Rab GTPase family has been extensively investigated. In this review, we summarize Rab GTPase- mediated membrane trafficking while focusing on the structures of Rab protein and Rab-effector complexes. This review provides detailed information that helps explain how the Rab GTPase family is involved in membrane trafficking. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview Roles of Rho GTPases in Intracellular Transport and Cellular Transformation
Int. J. Mol. Sci. 2013, 14(4), 7089-7108; doi:10.3390/ijms14047089
Received: 21 February 2013 / Revised: 4 March 2013 / Accepted: 12 March 2013 / Published: 28 March 2013
Cited by 18 | PDF Full-text (517 KB) | HTML Full-text | XML Full-text
Abstract
Rho family GTPases belong to the Ras GTPase superfamily and transduce intracellular signals known to regulate a variety of cellular processes, including cell polarity, morphogenesis, migration, apoptosis, vesicle trafficking, viral transport and cellular transformation. The three best-characterized Rho family members are Cdc42, [...] Read more.
Rho family GTPases belong to the Ras GTPase superfamily and transduce intracellular signals known to regulate a variety of cellular processes, including cell polarity, morphogenesis, migration, apoptosis, vesicle trafficking, viral transport and cellular transformation. The three best-characterized Rho family members are Cdc42, RhoA and Rac1. Cdc42 regulates endocytosis, the transport between the endoplasmic reticulum and Golgi apparatus, post-Golgi transport and exocytosis. Cdc42 influences trafficking through interaction with Wiskott-Aldrich syndrome protein (N-WASP) and the Arp2/3 complex, leading to changes in actin dynamics. Rac1 mediates endocytic and exocytic vesicle trafficking by interaction with its effectors, PI3kinase, synaptojanin 2, IQGAP1 and phospholipase D1. RhoA participates in the regulation of endocytosis through controlling its downstream target, Rho kinase. Interestingly, these GTPases play important roles at different stages of viral protein and genome transport in infected host cells. Importantly, dysregulation of Cdc42, Rac1 and RhoA leads to numerous disorders, including malignant transformation. In some cases, hyperactivation of Rho GTPases is required for cellular transformation. In this article, we review a number of findings related to Rho GTPase function in intracellular transport and cellular transformation. Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)
Open AccessReview RUFY, Rab and Rap Family Proteins Involved in a Regulation of Cell Polarity and Membrane Trafficking
Int. J. Mol. Sci. 2013, 14(3), 6487-6498; doi:10.3390/ijms14036487
Received: 31 December 2012 / Revised: 11 March 2013 / Accepted: 15 March 2013 / Published: 21 March 2013
Cited by 6 | PDF Full-text (204 KB) | HTML Full-text | XML Full-text
Abstract
Cell survival, homeostasis and cell polarity rely on the control of membrane trafficking pathways. The RUN domain (comprised of the RPIP8, UNC-14, and NESCA proteins) has been suggested to be implicated in small GTPase-mediated membrane trafficking and cell polarity. Accumulating evidence supports [...] Read more.
Cell survival, homeostasis and cell polarity rely on the control of membrane trafficking pathways. The RUN domain (comprised of the RPIP8, UNC-14, and NESCA proteins) has been suggested to be implicated in small GTPase-mediated membrane trafficking and cell polarity. Accumulating evidence supports the hypothesis that the RUN domain-containing proteins might be responsible for an interaction with a filamentous network linked to actin cytoskeleton and/or microtubules. In addition, several downstream molecules of PI3K are involved in regulation of the membrane trafficking by interacting with vesicle-associated RUN proteins such as RUFY family proteins. In this review, we summarize the background of RUN domain research with an emphasis on the interaction between RUN domain proteins including RUFY proteins (designated as RUN and FYVE domain-containing proteins) and several small GTPases with respect to the regulation of cell polarity and membrane trafficking on filamentous network Full article
(This article belongs to the Special Issue Regulation of Membrane Trafficking and Its Potential Implications)

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