Special Issue "Structure and Function of Membrane Receptors"

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A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membranes (Transport Processes)".

Deadline for manuscript submissions: closed (31 May 2015)

Special Issue Editor

Guest Editor
Dr. Christian Brix Folsted Andersen

Department of Biomedicine, Aarhus University, 8000 Aarhus C, Denmark
Website | E-Mail
Phone: +45 30 26 48 55
Fax: +45 87 15 02 01
Interests: membrane receptors; X-ray crystallography; hemoglobin scavenging; trypanosome parasites

Special Issue Information

Dear Colleagues,

The cell membrane is a semi-permeable barrier that surrounds the cell’s cytoplasm. Its function is to protect the integrity of the interior of the cell by allowing certain substances to enter the cell, while keeping others out. The major components of the cell membrane are phospholipids, which form a bilayer with the hydrophobic tails packed in the interior of the membrane and the hydrophilic head groups facing the cytoplasm and the extracellular fluid. Additional components in the membrane are cholesterol, glycolipids and proteins.

Membrane receptors are specialized protein molecules attached to or integrated into the cell membrane. Through interaction with specific ligands (e.g., hormones and neurotransmitters), the receptors facilitate communication between the cell and the extracellular environment. Receptors are also involved in translocation of substances (e.g., nutrients and waste products) across the membrane. These endocytic receptors bind specific ligands and, through invagination of the cell membrane, the ligands are imported into the interior of the cell.

This special issue of Membranes will focus on papers that characterize the structural and functional properties of membrane receptors and their interaction with ligands.

Dr. Christian Brix Folsted Andersen
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. 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 500 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
  • ligands
  • endocytosis
  • signaling
  • cell adhesion

Published Papers (3 papers)

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Research

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Open AccessArticle Flexibility in the Insulin Receptor Ectodomain Enables Docking of Insulin in Crystallographic Conformation Observed in a Hormone-Bound Microreceptor
Membranes 2014, 4(4), 730-746; doi:10.3390/membranes4040730
Received: 18 August 2014 / Revised: 18 September 2014 / Accepted: 5 October 2014 / Published: 10 October 2014
Cited by 2 | PDF Full-text (1546 KB) | HTML Full-text | XML Full-text
Abstract
Insulin binding to the insulin receptor (IR) is the first key step in initiating downstream signaling cascades for glucose homeostasis in higher organisms. The molecular details of insulin recognition by IR are not yet completely understood, but a picture of hormone/receptor interactions at
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Insulin binding to the insulin receptor (IR) is the first key step in initiating downstream signaling cascades for glucose homeostasis in higher organisms. The molecular details of insulin recognition by IR are not yet completely understood, but a picture of hormone/receptor interactions at one of the epitopes (Site 1) is beginning to emerge from recent structural evidence. However, insulin-bound structures of truncated IR suggest that crystallographic conformation of insulin cannot be accommodated in the full IR ectodomain due to steric overlap of insulin with the first two type III fibronectin domains (F1 and F2), which are contributed to the insulin binding-pocket by the second subunit in the IR homodimer. A conformational change in the F1-F2 pair has thus been suggested. In this work, we present an all-atom structural model of complex of insulin and the IR ectodomain, where no structural overlap of insulin with the receptor domains (F1 and F2) is observed. This structural model was arrived at by flexibly fitting parts of our earlier insulin/IR all-atom model into the simulated density maps of crystallized constructs combined with conformational sampling from apo-IR solution conformations. Importantly, our experimentally-consistent model helps rationalize yet unresolved Site Full article
(This article belongs to the Special Issue Structure and Function of Membrane Receptors)
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Review

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Open AccessReview Vitamin A Transport Mechanism of the Multitransmembrane Cell-Surface Receptor STRA6
Membranes 2015, 5(3), 425-453; doi:10.3390/membranes5030425
Received: 27 June 2015 / Accepted: 24 August 2015 / Published: 28 August 2015
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Abstract
Vitamin A has biological functions as diverse as sensing light for vision, regulating stem cell differentiation, maintaining epithelial integrity, promoting immune competency, regulating learning and memory, and acting as a key developmental morphogen. Vitamin A derivatives have also been used in treating human
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Vitamin A has biological functions as diverse as sensing light for vision, regulating stem cell differentiation, maintaining epithelial integrity, promoting immune competency, regulating learning and memory, and acting as a key developmental morphogen. Vitamin A derivatives have also been used in treating human diseases. If vitamin A is considered a drug that everyone needs to take to survive, evolution has come up with a natural drug delivery system that combines sustained release with precise and controlled delivery to the cells or tissues that depend on it. This “drug delivery system” is mediated by plasma retinol binding protein (RBP), the principle and specific vitamin A carrier protein in the blood, and STRA6, the cell-surface receptor for RBP that mediates cellular vitamin A uptake. The mechanism by which the RBP receptor absorbs vitamin A from the blood is distinct from other known cellular uptake mechanisms. This review summarizes recent progress in elucidating the fundamental molecular mechanism mediated by the RBP receptor and multiple newly discovered catalytic activities of this receptor, and compares this transport system with retinoid transport independent of RBP/STRA6. How to target this new type of transmembrane receptor using small molecules in treating diseases is also discussed. Full article
(This article belongs to the Special Issue Structure and Function of Membrane Receptors)
Open AccessReview Theoretical and Computational Studies of Peptides and Receptors of the Insulin Family
Membranes 2015, 5(1), 48-83; doi:10.3390/membranes5010048
Received: 26 August 2014 / Accepted: 28 January 2015 / Published: 11 February 2015
Cited by 2 | PDF Full-text (3699 KB) | HTML Full-text | XML Full-text
Abstract
Synergistic interactions among peptides and receptors of the insulin family are required for glucose homeostasis, normal cellular growth and development, proliferation, differentiation and other metabolic processes. The peptides of the insulin family are disulfide-linked single or dual-chain proteins, while receptors are ligand-activated transmembrane
[...] Read more.
Synergistic interactions among peptides and receptors of the insulin family are required for glucose homeostasis, normal cellular growth and development, proliferation, differentiation and other metabolic processes. The peptides of the insulin family are disulfide-linked single or dual-chain proteins, while receptors are ligand-activated transmembrane glycoproteins of the receptor tyrosine kinase (RTK) superfamily. Binding of ligands to the extracellular domains of receptors is known to initiate signaling via activation of intracellular kinase domains. While the structure of insulin has been known since 1969, recent decades have seen remarkable progress on the structural biology of apo and liganded receptor fragments. Here, we review how this useful structural information (on ligands and receptors) has enabled large-scale atomically-resolved simulations to elucidate the conformational dynamics of these biomolecules. Particularly, applications of molecular dynamics (MD) and Monte Carlo (MC) simulation methods are discussed in various contexts, including studies of isolated ligands, apo-receptors, ligand/receptor complexes and intracellular kinase domains. The review concludes with a brief overview and future outlook for modeling and computational studies in this family of proteins. Full article
(This article belongs to the Special Issue Structure and Function of Membrane Receptors)
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