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Advances in Membrane Proteins: From Structure to Function and Molecular...
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Advances in Membrane Proteins: From Structure to Function and Molecular Engineering

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins, Nucleic Acids and Carbohydrates".

Deadline for manuscript submissions: 31 December 2026 | Viewed by 3376

Special Issue Editors

Dr. Ximin Chi

E-Mail Website
Guest Editor
State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Science, Xiamen University, Xiamen, China
Interests: structural analysis and functional mechanism research of membrane proteins and protein complexes by cryo-electron microscopy
Dr. Renhong Yan

E-Mail Website
Guest Editor
Key University Laboratory of Metabolism and Health of Guangdong, Institute for Biological Electron Microscopy, Southern University of Science and Technology, Shenzhen 518055, China
Interests: membrane proteins; the structural and mechanistic investigation of physiologically and patho-physiologically important membrane proteins; key regulators for cholesterol metabolism; the heteromeric amino acid transporters

Special Issue Information

Dear Colleagues,

Based on the partitioning of phospholipid membranes for water-soluble reactions, living organisms can efficiently carry out their vital activities. The formation of the membrane is widely regarded as a hallmark of the emergence of life. Lipid-constituted membranes exist in almost all phyla of organisms, ranging from viruses, archaea, to prokaryotes and eukaryotes. The transport and signal transduction conducted by membrane proteins are of high importance for the harmonious arrangement of various living activities throughout the entire life cycle. Therefore, it is evident that membrane proteins, which establish the connections between different cell compartments and facilitate communication between organisms and their environments, are indispensable for nearly all living processes.

Structural biology decodes biological questions into their chemical basis, providing fundamental insights into the chemical basis of living activities. The technological leap in cryo-EM single-particle 3D reconstruction contributes to the progress in structural research of transmembrane proteins. Structural analysis of membrane proteins is the cornerstone for a comprehensive understanding of transmembrane biological processes, such as cell development and differentiation, immune response, metabolism, osmotic and ion homeostasis, and protein folding quality control, among others. It also reveals the molecular mechanisms of host defense, plant resilience, and membrane-based reactions, including photosynthesis and the respiratory chain. Moreover, membrane protein structure research facilitates rationalized protein design and molecular engineering, paving the way for promising prospects in efficient drug delivery, environmentally friendly material development, and ecological rehabilitation. However, the prominent scientific questions surrounding membrane proteins, including substrate/ligand recognition, conformational change in transport/activation, and dynamic complex assembly, remain challenging, even with the wide application of artificial intelligence in structure prediction. In this Special Issue, we collect original research articles and reviews on the advancements in the structural and functional study of membrane proteins. Research areas may include (but are not limited to) the following: the structural basis for the mechanisms of transmembrane living activities, new technologies and methodologies in experimental structure research and prediction, and innovation in molecular engineering and protein design.

We look forward to receiving your contributions.

Dr. Ximin Chi
Dr. Renhong Yan
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 250 words) can be sent to the Editorial Office for assessment.

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. Biomolecules 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

  • membrane transport
  • transmembrane signaling
  • membrane protein complex
  • membrane-based reactions
  • membrane and protein interaction
  • regulation of membrane proteins
  • membrane protein design
  • membrane protein engineering

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Published Papers (3 papers)

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Research

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16 pages, 3664 KB  
Article
LRP1 Interacts with the Rift Valley Fever Virus Glycoprotein Gn via a Calcium-Dependent Multivalent Electrostatic Mechanism
by Haonan Yang, Haojin Chen, Wanyan Jiang and Renhong Yan
Biomolecules 2026, 16(1), 14; https://doi.org/10.3390/biom16010014 - 21 Dec 2025
Viewed by 981
Abstract
The Rift Valley fever virus (RVFV) is a highly pathogenic, mosquito-borne zoonotic virus that poses a significant risk to livestock, human health, and global public health security. Although RVFV is classified by the World Health Organization (WHO) as a priority pathogen with epidemic [...] Read more.
The Rift Valley fever virus (RVFV) is a highly pathogenic, mosquito-borne zoonotic virus that poses a significant risk to livestock, human health, and global public health security. Although RVFV is classified by the World Health Organization (WHO) as a priority pathogen with epidemic potential, no licensed vaccines or effective antiviral therapies are currently available. A limited understanding of the molecular mechanisms of RVFV entry has hindered therapeutic development. Here, we elucidate the molecular basis by which the RVFV envelope glycoprotein Gn recognizes its receptor, low-density lipoprotein receptor-related protein 1 (LRP1). Bio-layer interferometry (BLI) demonstrates that full-length LRP1 directly binds the head domain of Gn with nanomolar affinity in a Ca2+-dependent manner. Both LRP1 clusters II (CL II) and IV (CL IV) independently interact with Gn, with CL IV exhibiting stronger affinity, indicating a multivalent recognition mode. Structural modeling using AlphaFold 3 reveals pronounced charge complementarity between basic residues on Gn and acidic, Ca2+-coordinated pockets within LRP1. Mutations in key acidic residues in CL IV greatly reduced Gn binding, confirming the essential roles of Ca2+ coordination and electrostatic interactions. Collectively, our findings define a Ca2+-stabilized, electrostatically driven mechanism for RVFV Gn recognition by LRP1, providing molecular insight into viral entry and a structural framework for the rational design of vaccines and antiviral therapeutics. Full article
(This article belongs to the Special Issue Advances in Membrane Proteins: From Structure to Function and Molecular Engineering)
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26 pages, 3377 KB  
Article
Charge Neutralization During Peptide Transport in the Bacterial SecYEG Translocon
by Laura Nübl, Ekaterina Sobakinskaya and Frank Müh
Biomolecules 2025, 15(10), 1442; https://doi.org/10.3390/biom15101442 - 12 Oct 2025
Viewed by 998
Abstract
The driving force behind protein translocation across the cell membrane is not yet fully understood. In bacteria, there is an electrochemical potential across the cell membrane, which can interact with charged residues in the translocation substrate. In this study, the protonation states of [...] Read more.
The driving force behind protein translocation across the cell membrane is not yet fully understood. In bacteria, there is an electrochemical potential across the cell membrane, which can interact with charged residues in the translocation substrate. In this study, the protonation states of lysine and glutamate, serving as test residues in a peptide translocating across the bacterial channel SecYEG, are investigated by applying Poisson–Boltzmann continuum electrostatic free energy calculations and Monte Carlo titrations to snapshots of molecular dynamics (MD) simulations. A clear shift in protonation probability towards the uncharged state is found for both test residues as they move deeper into the channel. Thus, charge neutralization occurs irrespective of whether the original charge of the test residue is positive (lysine) or negative (glutamate). Electrostatic interactions of acidic and basic residues of SecYEG with the peptide cancel out. The main determinants of the test residue’s protonation state are the dielectric properties of its surroundings and interactions with non-titrating charges in the channel. Crucially, the membrane protein—including its water-filled pore—is assigned a low dielectric constant. The results are discussed in the context of the limitations inherent to continuum electrostatics and MD simulations with fixed protonation states. Full article
(This article belongs to the Special Issue Advances in Membrane Proteins: From Structure to Function and Molecular Engineering)
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Review

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31 pages, 1695 KB  
Review
The Landscape of SERCA2 in Cardiovascular Diseases: Expression Regulation, Therapeutic Applications, and Emerging Roles
by Jianmin Wu, Mengting Liao, Tengkun Dai, Guiyan Liu, Jiayi Zhang, Yiling Zhu, Lin Xu and Juanjuan Zhao
Biomolecules 2026, 16(2), 247; https://doi.org/10.3390/biom16020247 - 4 Feb 2026
Viewed by 937
Abstract
Driven by rapid socioeconomic progress and changing lifestyles, the global burden of cardiovascular diseases (CVDs) continues to escalate, with surging morbidity and mortality rates imposing a severe threat to public health. Clinical treatments are focused on the alleviation of treatments, highlighting the need [...] Read more.
Driven by rapid socioeconomic progress and changing lifestyles, the global burden of cardiovascular diseases (CVDs) continues to escalate, with surging morbidity and mortality rates imposing a severe threat to public health. Clinical treatments are focused on the alleviation of treatments, highlighting the need for a deeper understanding of CVDs pathogenesis and the development of targeted therapies. Recent studies have identified imbalances in intracellular Ca2+ homeostasis as a key pathological mechanism in the progression of CVDs. Notably, sarcoplasmic/endoplasmic reticulum Ca2+-ATPase 2 (SERCA2), a membrane protein encoded by the ATP2A2 gene and ranging from 97 to 115 kDa in molecular weight, plays a pivotal role in regulating intracellular Ca2+ levels. Extensive evidence links abnormal SERCA2 function to various CVDs, including heart failure, cardiac hypertrophy, atherosclerosis, and diabetic cardiomyopathy. This review systematically explores the regulatory mechanisms of SERCA2 expression and its functional regulation—including transcriptional regulation, post-translational modifications, and protein–protein interactions—and further investigates its pathological roles in cardiovascular diseases as well as its potential as a therapeutic target. By synthesizing current knowledge, this article aims to provide new insights for future basic research and establish a theoretical foundation for clinical applications. Full article
(This article belongs to the Special Issue Advances in Membrane Proteins: From Structure to Function and Molecular Engineering)
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