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Stress-Activated Molecular Remodeling: Lipids, Chaperones, and the Cytoskeleton
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Stress-Activated Molecular Remodeling: Lipids, Chaperones, and the Cytoskeleton

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

Deadline for manuscript submissions: 20 May 2026 | Viewed by 1453

Special Issue Editor

Dr. Nikolas Nikolaidis

E-Mail Website
Guest Editor
Department of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, California State University Fullerton, Fullerton, CA 92831, USA
Interests: heat shock response; membrane-associated heat shock proteins; protein–lipid interactions
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Cells respond to acute and chronic stress through the rapid and coordinated remodeling of key molecular systems, including membranes, cytoskeletal networks, and protein homeostasis machinery. This Special Issue will focus on the dynamic interplay between lipid signaling, cytoskeletal reorganization, and chaperone activity during cellular stress responses, particularly emphasizing their implications for human health and disease. We welcome studies that investigate how stress triggers changes in membrane composition, lipid–protein interactions, cytoskeletal architecture, and proteostasis—and how these processes contribute to pathological conditions such as cancer, neurodegeneration, infection, and inflammatory disorders. By highlighting emerging research on the crosstalk between structural and functional elements of stressed cells, this Special Issue aims to bridge basic molecular mechanisms with translational insights, bringing together perspectives from biochemistry, cell biology, biophysics, and disease modeling.

We invite original research articles and reviews exploring how cells dynamically remodel molecular systems in response to stress. This Special Issue focuses on the interplay between lipid signaling, membrane dynamics, cytoskeletal reorganization, and chaperone function, and how these processes contribute to cellular adaptation, survival, and disease. Submissions with mechanistic insights or translational relevance to conditions such as cancer, neurodegeneration, infection, or inflammation are especially welcome.

Topics include (but are not limited to) the following: 

- Membrane and lipid remodeling under stress;

- Chaperone function and proteostasis;

- Cytoskeletal dynamics and mechano-signaling;

- Membrane–protein interactions and trafficking;

- Stress responses in human disease models.

Prof. Dr. Nikolas Nikolaidis
Guest Editor

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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • cellular stress response
  • molecular remodeling
  • lipid signaling
  • membrane dynamics
  • cytoskeletal reorganization
  • chaperones
  • heat shock proteins
  • proteostasis
  • membrane–protein interactions
  • stress-induced trafficking
  • mechano-transduction
  • cell survival signaling

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Published Papers (2 papers)

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19 pages, 7876 KB  
Article
YB-1 AP–CSD Forms Cross-β Amyloid Fibrils Without Secondary-Structure Conversion In Vitro
by Maria A. Timchenko, Oxana V. Galzitskaya, Alexander V. Chulkov, Ilya V. Likhachev, Anna V. Glyakina, Maxim V. Molchanov, Nikolay V. Molochkov, Nikita V. Penkov, Liya G. Bobyleva, Vitalii A. Balobanov, Alexander Ye. Yegorov, Sergey G. Guryanov, Alexey D. Nikulin, Dmitry N. Lyabin, Ivan M. Vikhlyantsev and Alexander G. Bobylev
Int. J. Mol. Sci. 2026, 27(8), 3553; https://doi.org/10.3390/ijms27083553 - 16 Apr 2026
Viewed by 293
Abstract
The central role of YB-1 in messenger ribonucleoprotein particle (mRNP) metabolism and stress-granule biology highlights the importance of defining the determinants of its self-assembly. YB-1 fibrillogenesis has been attributed primarily to the cold shock domain (CSD). Here, we show that the YB-1 fragment [...] Read more.
The central role of YB-1 in messenger ribonucleoprotein particle (mRNP) metabolism and stress-granule biology highlights the importance of defining the determinants of its self-assembly. YB-1 fibrillogenesis has been attributed primarily to the cold shock domain (CSD). Here, we show that the YB-1 fragment spanning residues 1–129 (AP–CSD) form amyloid fibrils under near-physiological ionic strength (0.12–0.15 M KCl). Fibrillization proceeds without a pronounced exponential growth phase and increases approximately linearly over 45–50 h. Far-UV circular dichroism (CD) and attenuated total reflection Fourier-transform infrared spectroscopy (ATR-FTIR) indicate no substantial change in overall secondary-structure content during aggregation. In parallel, 1H nuclear magnetic resonance (NMR) spectroscopy reveals the depletion of soluble species, and oriented fiber X-ray diffraction displays the hallmark cross-β reflections at approximately 4.7 Å and 10 Å. The prolonged formation time implies an activation barrier that is unlikely to require global refolding. Instead, it may reflect early association events such as dimerization or other local rearrangements required for primary nucleation, followed by consolidation into stable intermolecular contacts. Aggregation that preserves a largely native-like fold while establishing cross-β order may reduce recognition by cellular quality-control systems that preferentially target globally unfolded or strongly destabilized states. This provides a plausible framework for how YB-1 derived assemblies could persist under stress and during age-associated proteostasis decline. Full article
(This article belongs to the Special Issue Stress-Activated Molecular Remodeling: Lipids, Chaperones, and the Cytoskeleton)
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15 pages, 2053 KB  
Article
Pyrroloquinoline Quinone Protects Against Light-Induced Retinal Damage in Association with the Suppression of c-Fos Signalling
by Hinata Ozawa, Eriko Sugano, Kitako Tabata, Taira Kakizaki, Akimune Sato, Yoshihiro Takai, Kohei Sone, Miwako Shidomi, Yuki Ishii, Akito Saito, Kentaro Totuka, Taku Ozaki, Tomokazu Fukuda, Lanlan Bai and Hiroshi Tomita
Int. J. Mol. Sci. 2026, 27(4), 1929; https://doi.org/10.3390/ijms27041929 - 17 Feb 2026
Viewed by 644
Abstract
Age-related macular degeneration (AMD) is a progressive retinal disorder characterised by oxidative stress and inflammation. Although pyrroloquinoline quinone (PQQ) has been reported to exert neuroprotective effects, its specific efficacy in in vivo models of AMD pathophysiology has not yet been elucidated. In this [...] Read more.
Age-related macular degeneration (AMD) is a progressive retinal disorder characterised by oxidative stress and inflammation. Although pyrroloquinoline quinone (PQQ) has been reported to exert neuroprotective effects, its specific efficacy in in vivo models of AMD pathophysiology has not yet been elucidated. In this study, we evaluated the protective effects of PQQ against all-trans-retinal (ATR)-induced cytotoxicity in ARPE-19 cells and light-induced photoreceptor degeneration in rats. Pretreatment of ARPE-19 cells with PQQ dose-dependently mitigated ATR-induced cytotoxicity. In the in vivo model, rats received a single intraperitoneal injection of PQQ (2 or 5 mg/kg) 1 h prior to 1000-lux light exposure. Retinal function and morphology were evaluated by electroretinography and haematoxylin–eosin staining, respectively. The 5 mg/kg PQQ group retained significantly greater retinal function than the vehicle group at 3 days postexposure and demonstrated significant preservation of the outer nuclear layer at 7 days postexposure, indicating the suppression of photoreceptor cell death. Western blot analysis detected the dose-dependent suppression of light-induced c-Fos upregulation following PQQ treatment. These findings suggest that the protective effect of PQQ against phototoxic damage is associated with the suppression of c-Fos signalling, thus lending support to the further investigation of PQQ as a potential therapeutic agent for AMD. Full article
(This article belongs to the Special Issue Stress-Activated Molecular Remodeling: Lipids, Chaperones, and the Cytoskeleton)
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