Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
4.4
4.2
Journals
Membranes
Special Issues
Recent Progress in Protein Regulation by Membranes: Structure, Function, and...
share announcement

Recent Progress in Protein Regulation by Membranes: Structure, Function, and Dynamics

A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membrane Composition and Structures".

Deadline for manuscript submissions: 30 April 2024 | Viewed by 1769

Special Issue Editors

Dr. Agata Nawrotek

E-Mail Website
Guest Editor
LBPA, UMR8113 CNRS, Ecole Normale Supérieure Paris-Saclay, Université Paris- Saclay, 91190 Gif-sur-Yvette, France
Interests: membrane proteins; structural biology; TIRF; optogenetics
Dr. Marc Baaden

E-Mail Website
Guest Editor
Laboratoire de Biochimie Théorique, CNRS, Université Paris Cité, 13 rue Pierre et Marie, Curie, F-75005 Paris, France
Interests: molecular dynamics; membrane proteins; artificial water channels; ion channels; molecular modeling of complex membrane systems including enveloped viruses; artificial water channels for desalination purposes and membrane fusion machinery

Special Issue Information

Dear Colleagues,

We are excited to announce a call for submissions to our Special Issue, which aims to explore the intricate molecular mechanisms that govern cellular processes at the membrane interface.

Cellular membranes provide a dynamic platform for a plethora of cellular processes, including signal transduction, energy transduction, and intercellular communication. This Special Issue will particularly highlight research on the dynamics of peripheral protein networks, the influence of membranes on protein structure and function, and the impact proteins have on the properties of membranes themselves. Your contributions may include original research articles or comprehensive reviews. Potential topics of interest include, but are not limited to, the following:

  • Structure–Function Relationships at Membrane Interfaces: Articles unravelling the complex interactions between proteins and membranes and their roles in crucial cellular functions, including signaling pathways, trafficking, cytoskeleton dynamics, and energy transformations.
  • Insights into Protein–Membrane Dynamics: Studies that elucidate the fundamental principles of bidirectional dynamic protein–lipid interactions and multi-protein dynamic network interplay on membranes, using biophysical approaches or molecular modeling.
  • Technological Advances and Applications: Insights from studies of protein–membrane interactions can have significant implications for biotechnological advancements. Contributions may include research with applications in developing cutting-edge biosensors, bioenergy devices, and other biotechnological innovations.

We look forward to receiving submissions that not only advance our scientific knowledge but which also have the potential to catalyze technological breakthroughs in this fascinating field.

Dr. Agata Nawrotek
Dr. Marc Baaden
Guest Editors

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. Membranes 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 2700 CHF (Swiss Francs). 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

  • protein–membrane interactions
  • membrane peripheral proteins
  • membrane dynamics
  • allosteric regulation
  • lipid binding pocket
  • small GTPases
  • transmembrane receptors

Published Papers (1 paper)

Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

12 pages, 2102 KiB  
Article
The MA Helix Is Important for Receptor Assembly and Function in the α4β2 nACh Receptor
by Dorottya I. Fricska, Susanne M. Mesoy and Sarah C. R. Lummis
Membranes 2023, 13(12), 891; https://doi.org/10.3390/membranes13120891 - 29 Nov 2023
Viewed by 1566
Abstract
Pentameric ligand-gated ion channels (pLGICs) are expressed throughout the central and peripheral nervous systems of vertebrates and modulate many aspects of human health and disease. Recent structural and computational data indicate that cation-selective pLGICs contain a long helical extension (MA) of one of [...] Read more.
Pentameric ligand-gated ion channels (pLGICs) are expressed throughout the central and peripheral nervous systems of vertebrates and modulate many aspects of human health and disease. Recent structural and computational data indicate that cation-selective pLGICs contain a long helical extension (MA) of one of the transmembrane helices. The MA helix has been shown to affect both the membrane expression of, and ion conductance levels through, these pLGICs. Here we probe the functional effects of 68 mutations in the MA region of the α4β2 nicotinic acetylcholine receptor (nAChR), using a voltage-sensitive membrane dye and radioligand binding to measure receptor function and expression/assembly. We found seven alanine mutations in a stretch of the MA helix that prevent correct receptor folding and/or assembly, as evidenced by the lack of both function and ligand binding. A further two alanine mutations resulted in receptors that were capable of binding ligand but showed no functional response, and we propose that, in these mutants, ligand binding is insufficient to trigger channel opening. The data clarify the effect of the MA helix, and as the effects of some of our mutations in the α4β2 nAChR differ from the effects of equivalent mutations in other cation-selective pLGICs, we suggest that residues in the MA helix may play subtly different roles in different receptors. Full article
(This article belongs to the Special Issue Recent Progress in Protein Regulation by Membranes: Structure, Function, and Dynamics)
►▼ Show Figures

Graphical abstract

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-1
Back to TopTop