Special Issue "Trafficking of Membrane Receptors"

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A special issue of Membranes (ISSN 2077-0375).

Deadline for manuscript submissions: closed (31 May 2014)

Special Issue Editors

Guest Editor
Dr. Morten S. Nielsen
Institut for Medicinsk Biokemi, Ole Worms Allé, Bygn. 170, Universitetsparken, 8000 Århus C, Denmark
Website: http://biomed.au.dk/en/research/researchers-and-research-laboratories/n-o/nielsen-morten/
E-Mail: mn@biokemi.au.dk
Phone: +45 87167794
Fax: +45 861 31160
Interests: receptors; endocytosis; intracellular trafficking; lipoprotein; lipase

Guest Editor
Prof. Dr. Oddmund Bakke
Department of Molecular Biosciences, University of Oslo, Oslo 0316, Norway
Website: http://www.med.uio.no/cir/english/research/groups/bakke/
E-Mail: oddmund.bakke@imbv.uio.no
Phone: +47 2285 5787

Special Issue Information

Dear Colleagues,

Recently, the Nobel Prize in Physiology and Medicine was awarded to Dr. James E. Rothman, Dr. Randy W. Schekman and Dr. Thomas C. Südhof for their ground-breaking research concerning the regulation of vesicular traffic in eukaryotic cells. The vesicular system is used by membrane receptors for cellular trafficking; such trafficking includes exocytosis, endocytosis, transport in the endo-lysosomal system. After the receptors are incorporated into vesicles, subcellular trafficking including fusion, fission between vesicles, tubular structures from trans Golgi-network and endosomes and these complex events are all mediated by several adaptor and coat proteins (e.g., the Adaptor Complexes 1 to 4, the retromer complex, RAB proteins, and many others). Furthermore, active signaling within the endosomal pathway is of special interest for us. Also, asymmetric trafficking in polarized cells (e.g., epithelial and endothelial cells and neurons), adds an additional layer of complexity.

For this Special Issue of Membranes—“Trafficking of Membrane Receptors”, we encourage you to submit manuscripts discussing how the trafficking of recycling, retrograde-sorted, and other receptors is regulated in cells.

Dr. Morten S. Nielsen
Prof. Dr. Oddmund Bakke
Guest Editors

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. Membranes is an international peer-reviewed Open Access quarterly 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 300 CHF (Swiss Francs). English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.


Keywords

  • membrane receptors
  • anterograde traffic
  • retrograde traffic
  • endocytosis
  • exocytosis
  • adaptor proteins
  • coat proteins

Published Papers (11 papers)

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Displaying article 1-11
p. 642-677
by ,  and
Membranes 2014, 4(4), 642-677; doi:10.3390/membranes4040642
Received: 8 July 2014; in revised form: 27 August 2014 / Accepted: 16 September 2014 / Published: 6 October 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
p. 630-641
by ,  and
Membranes 2014, 4(3), 630-641; doi:10.3390/membranes4030630
Received: 10 June 2014; in revised form: 5 September 2014 / Accepted: 9 September 2014 / Published: 16 September 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
p. 608-629
by  and
Membranes 2014, 4(3), 608-629; doi:10.3390/membranes4030608
Received: 28 May 2014; in revised form: 2 August 2014 / Accepted: 18 August 2014 / Published: 3 September 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
p. 565-595
by , ,  and
Membranes 2014, 4(3), 565-595; doi:10.3390/membranes4030565
Received: 6 July 2014; in revised form: 4 August 2014 / Accepted: 12 August 2014 / Published: 20 August 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
p. 525-564
by , , ,  and
Membranes 2014, 4(3), 525-564; doi:10.3390/membranes4030525
Received: 16 June 2014; in revised form: 11 July 2014 / Accepted: 8 August 2014 / Published: 19 August 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
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p. 469-490
by , ,  and
Membranes 2014, 4(3), 469-490; doi:10.3390/membranes4030469
Received: 16 June 2014; in revised form: 17 July 2014 / Accepted: 25 July 2014 / Published: 8 August 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
p. 424-446
by  and
Membranes 2014, 4(3), 424-446; doi:10.3390/membranes4030424
Received: 27 May 2014; in revised form: 1 July 2014 / Accepted: 22 July 2014 / Published: 6 August 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
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p. 388-413
by ,  and
Membranes 2014, 4(3), 388-413; doi:10.3390/membranes4030388
Received: 5 June 2014; in revised form: 3 July 2014 / Accepted: 22 July 2014 / Published: 31 July 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
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p. 333-355
by ,  and
Membranes 2014, 4(3), 333-355; doi:10.3390/membranes4030333
Received: 31 May 2014; in revised form: 23 June 2014 / Accepted: 1 July 2014 / Published: 11 July 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
p. 356-371
by  and
Membranes 2014, 4(3), 356-371; doi:10.3390/membranes4030356
Received: 26 May 2014; in revised form: 28 June 2014 / Accepted: 2 July 2014 / Published: 11 July 2014
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(This article belongs to the Special Issue Trafficking of Membrane Receptors)
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p. 302-318
by ,  and
Membranes 2014, 4(3), 302-318; doi:10.3390/membranes4030302
Received: 29 May 2014; in revised form: 24 June 2014 / Accepted: 25 June 2014 / Published: 3 July 2014
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of Paper: Review
Title: Role of Phospholipase D in G-protein Coupled Receptor Function
Author: Lars-Ove Brandenburg
Affiliation: Department of Anatomy and Cell Biology, RWTH Aachen University, Wendlingweg 2, 52074 Aachen, Germany; E-Mail: lbrandenburg@ukaachen.de
Abstract: Agonist exposure of many G-protein coupled receptors induces a rapid receptor phosphorylation and uncoupling from G-proteins. Resensitization of these desensitized receptors requires endocytosis and subsequent dephosphorylation. Several works shows the involvement of phospholipid-specific phosphodiesterase phospholipase D (PLD) in the receptor endocytosis and recycling of many G-protein coupled receptors e.g. opioid, formyl or dopamine receptors. The PLD hydrolyzes the headgroup of a phospholipid, generally phosphatidylcholine (PC) to phosphatidic acid (PA) and choline and is assumed to play an important function in cell regulation and receptor trafficking. The two mammalian PLD isoforms 1 and 2 are regulated by protein kinases and GTP binding proteins of the ADP-ribosylation and Rho families. Mammalian and yeast PLD are also potently stimulated by phosphatidylinositol 4,5-bisphosphate. The PA product is an intracellular lipid messenger. PLD and PA activities are implicated in a wide range of physiological processes and diseases including inflammation, diabetes, oncogenesis or neurodegeneration. This review discusses the characterization, structure, regulation of PLD in the context of membrane located G-protein coupled receptor function.

Type of Paper: Review
Title: Road not Taken: Which Way to Chose from the TGN to the Plasma Membrane?
Author: Anne Spang
Affiliation: Biozentrum, Growth & Development, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland; E-Mail: anne.spang@unibas.ch
Abstract: The trans-Golgi network functions in the distribution of cargo into different transport vesicles that are destined to the endosomes, lysosomes and the plasma membrane. Over the years it became clear that there are at least two, if not more, transport pathways promoting plasma membrane localization of proteins. In spite of the importance temporal and spatial control of protein localization at the plasma membrane, the regulation of sorting into and the formation of different transport containers are still poorly understood. This review summarizes the current knowledge about the different transport pathway and discusses concepts of regulation and sorting at the TGN.

Type of Paper: Review
Title: Intracellular Trafficking of Antisense and siRNA Oligonucleotides
Author: Rudy Juliano
Affiliation: UNC Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, NC 27599, USA; E-Mail: rudy_juliano@med.unc.edu
Abstract: One of the major limitations on the therapeutic use of antisense and siRNA oligonucleotides is inefficient delivery to their sites of action in the cytosol or nucleus. It is clear that the pathways of cellular uptake and intracellular trafficking of oligonucleotides can strongly influence their pharmacological actions. Here we review current information on the basic processes of subcellular trafficking of oligonucleotides in the context of the implications for therapy.

Type of Paper: Review
Title:
Endocytic Receptor Megalin and its Associated Proteins in Proximal Tubule Epithelial Cells
Author:
Akihiko Saito
Affiliation:
Department of Applied Molecular Medicine, Niigata University Graduate School of Medical and Dental Sciences, 1-757 Asahimachi-dori, Chuo-ku, Niigata, 951-8510, Japan; E-Mail: akisaito@med.niigata-u.ac.jp
Abstract:
Receptor-mediated endocytosis is an important function of renal proximal tubule epithelial cells (PTECs) to reabsorb and metabolize proteins and other substances in glomerular filtrates. The function is involved in the conservation of nutrients, including carrier-bound vitamins and trace elements. Impairment of the process results in a loss of such substances and development of proteinuria, an important clinical sign of kidney disease and a risk marker for cardiovascular disease. Megalin, a member of the LDL receptor gene family, is a multiligand receptor expressed at clathrin-coated pits of PTECs and plays a central role in the endocyotic functions. Megalin interacts with various intracellular adaptor proteins for intracellular trafficking and cooperates with other membrane molecules such as cubilin-amnionless complex. Megalin and cubilin-amnionless complex may be involved in uptake of some toxic substances into PTECs, participating in the development of kidney diseases. Megalin is excreted into urine in soluble and insoluble forms, which are both being used as clinical biomarkers. Studies of megalin and its associated molecules will be useful for the future development of novel strategies for diagnosis and treatment of kidney diseases.

Type of Paper: Review
Title:
Review of the Influence of Auxiliary Subunits on the Forward Trafficking of AMPA Subtype Glutamate Receptors
Author
s: Simon Koesters 1,2,3 and Michael Hollmann 1
Affiliation:
1 Department of Biochemistry I—Receptorbiochemistry, Ruhr-University Bochum, Germany; E-Mail: Simon.Koesters@ruhr-uni-bochum.de
2
Graduate School of Chemistry and Biochemistry (GSCB), Ruhr-University Bochum, Germany
3
RUB Research School Plus, Ruhr-University Bochum, Germany
Abstract:
Ionotropic glutamate receptors (iGluR) are responsible for a mayor part of the excitatory signal transmission in the central nervous system (CNS). The iGluR protein family, based on pharmacological properties and sequence homologies, is subdivided into several different subclasses including NMDA receptors (GluN), AMPA receptors (GluA), kainate receptors (GluK), and delta receptors (GluD). Among these subclasses AMPA receptors are responsible for modifying the synaptic strength via fast regulation and relocation of AMPA receptors at the postsynaptic density (PSD) during plasticity-generating events such as long term depression (LTD) and long term potentiation (LTP). Critically important for these properties are auxiliary subunits such as the transmembrane AMPA receptor regulatory proteins (TARPs). However, within the last decade many additional auxiliary subunits of AMPA receptors have been discovered, including the cornichons (CNIH2/-3), CKAMP44, the SynDig protein family, SOL-1/-2, and GSG-1L. These proteins modify the electrophysiological and pharmacological properties of the receptor and some of them are responsible for the transport of the receptor to the cell membrane and the localization at the PSD of the synapse. In this review we are focusing on these interactions and the influence of auxiliary subunits on the trafficking and the localization of AMPA receptors in glutamatergic synapses.

Type of Paper: Review
Title: Calreticulin: Roles on Cell-Surface Protein Expression
Authors: Yue Jiang and Hiroaki Matsunami*
Affiliation: Department of Molecular Genetics and Microbiology and Department of Neurobiology, Duke Institute for Brain Sciences, Duke University Medical Center, Box 3054, 264 CARL Bldg., 213 Research Dr., Durham, NC 27710, USA; E-Mail: hiroaki.matsunami@duke.edu
Abstract: In order to perform their designated functions, proteins require precise subcellular localizations. This is especially true for cell-surface proteins, such as receptors and channels: they are able to transducer signals between the interior and exterior of the cell only when properly targeted to the cell membrane. Calreticulin is a multi-functional chaperone protein involved in protein folding, maturation and trafficking. However, evidence has been accumulating that calreticulin can also negatively regulate the surface expression of certain receptors and channels. For these instances, depletion of calreticulin enhances their cell-surface expression and function. In this review, we discuss the role of calreticulin with focus on its negative effects on the expression of cell-surface proteins.

Type of Paper: Article
Title: KLHL1 Promotes Recycling of Voltage-Gated T-type Channel CaV3.2 to the Plasma Membrane
Author: Erika Piedras-Rentería
Affiliation: Department of Cellular and Molecular Physiology, Neuroscience Institute, Stritch School of Medicine, Loyola University Chicago, Maywood, IL 60153, USA; E-Mail: erikapiedras@me.com

Type of Paper: Review
T
itle: Trafficking of Kainate Receptors
Authors:
Steffen Pahl 1,2,3,* and Michael Hollmann 1,2
Affiliation
s: 1 Department of Biochemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, Germany; E-Mail: steffen.pahl@rub.de
2
International Graduate School of Neuroscience, Ruhr University Bochum, Germany
3
Ruhr University Research School, Ruhr University Bochum
Abstract:
Ionotropic glutamate receptors (iGluRs) mediate the vast majority of excitatory neurotransmission in the central nervous system of vertebrates. In the protein family of iGluRs, kainate receptors (KARs) comprise the probably least well understood receptor class. Although KARs act as key players in the regulation of synaptic network activity, many properties and functions of these proteins remain elusive until now. Especially the precise pre-, extra-, and postsynaptic localization of KARs plays an important and at the same time critical role for neuronal function, and a disbalanced localization of KARs would ultimately lead to disregulated neuronal excitability.
Recently, important advances in the understanding of the regulation of surface expression, function, and agonist-dependent endocytosis of KARs have been achieved. For example, post-translational modifications like PKC-mediated phosphorylation and SUMOylation have been reported to critically influence surface expression and endocytosis, while newly discovered auxiliary proteins were shown to shape the function of KARs.
This review will mainly focus on the mechanisms involved in surface expression and endocytosis of the receptors, with an emphasis on data that has been published since 2010.

Type of Paper: Review
Title:
The Endocytic Trafficking of Membrane-Bound Cargo: A Flotillin Point of View
Authors:
Melanie Meister and Ritva Tikkanen *
Affiliation:
Institute of Biochemistry, University of Giessen, Giessen, Germany; E-Mail: Ritva.Tikkanen@biochemie.med.uni-giessen.de
Abstract: The ubiquitous and highly conserved flotillin proteins, flotillin-1 and flotillin-2, have been shown to be involved in various cellular processes such as cellular adhesion, signal transduction through receptor tyrosine kinases as well as in cellular trafficking pathways. Due to the fact that flotillins are acylated and form hetero-oligomers, they constitutively associate with cholesterol-enriched lipid microdomains. In the recent years, such microdomains have been appreciated as platforms that participate in endocytosis and other cellular trafficking steps. This review summarizes the current findings on the role of flotillins in cargo endocytosis and endosomal trafficking events. We will discuss the proposed function of flotillins in endocytosis in the light of recent findings that point towards a role for flotillins in a step that precedes the actual endocytosis of cargo molecules. Recent findings have also revealed that flotillins may be important for endosomal sorting and recycling of specific cargo molecules. In addition to these aspects, the cellular trafficking pathway of flotillins themselves as potential cargo in the context of growth factor stimulation will be dissected.

Last update: 16 April 2014

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