98%
921
2 minutes
20
Lipid rafts (LRs) are relatively well-ordered functional microdomains in cell membranes and play an irreplaceable role in physiological processes as a transduction platform for multiple signaling pathways. Due to their small size and high spatiotemporal dynamics, it is difficult to perform lipid raft-localized biomolecule imaging on the surface of living cells. Here, we report a DNA nanotechnology-based platform for reversible manipulation and localized analysis of lipid rafts, which consists of two modules: "patching and coding probe pair" and "fishing probe". The probe pair is generated by modifying two different sets of connectable DNA structures on a lipid raft-specific protein. After recognizing lipid rafts, the two probes in close proximity are linked by a DNA ligase reaction to form a lipid raft identity (LR-ID) code. The LR-ID strand patches and stabilizes the lipid raft structure. Interestingly, the raft patches formed can be depatched by restriction endonucleases, providing the first reversible manipulation of the lipid raft structure in living cells. We also designed a "fishing probe" with a DNA hairpin structure using an aptamer that can specifically bind to the target. The probe can cascade the reaction to two input signals "LR-ID" and "target protein" to generate an "off-on" fluorescence switch, allowing imaging and dynamic monitoring of target proteins localized in lipid rafts. By encoding arbitrary targets (in the case of glycans) in lipid rafts, we have created a universal lipid raft-localized imaging platform. This work provides an integrated analytical and manipulative platform to reveal lipid rafts and associated signaling pathways at the molecular level.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11503886 | PMC |
http://dx.doi.org/10.1021/cbmi.3c00109 | DOI Listing |
Data Brief
October 2025
Research and Development Centre, Regional Specialist Hospital, ul. Kamieńskiego 73a, 51-124, Wrocław, Poland.
Flotillin-binding protein networks serve as scaffolds, organizing lipid rafts and facilitating the recruitment of other raft-associated proteins such as receptors and downstream signaling molecules to regulate various intracellular pathways, including those involved in cell proliferation, migration, and endocytosis. Flotillins belong to the SPFH (stomatin/prohibitin/flotillin/HflK/C) domain-containing protein family, also known as the prohibitin homology (PHB) domain, which enables membrane association via acylation and hydrophobic hairpin motifs that anchor them to the inner leaflet of the plasma membrane. The functional diversity of flotillin proteins within membrane microdomains primarily stems from their interactions with other proteins.
View Article and Find Full Text PDFiScience
September 2025
Laboratory of Health Chemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aoba, Aramaki, Aoba-ku, Sendai 980-8578, Japan.
Fatty acids (TFAs) have been associated with various inflammatory diseases, including atherosclerosis and metabolic syndrome, such as metabolic dysfunction-associated steatotic liver disease (MASLD)/metabolic dysfunction-associated steatohepatitis (MASH). However, the underlying mechanism remains unclear. Here, we show that in response to DNA damage, elaidic acid (EA), a most common TFA, amplifies interleukin-1 receptor (IL-1R) signaling, leading to the promotion of cellular senescence and senescence-associated secretory phenotype (SASP).
View Article and Find Full Text PDFJ Clin Invest
September 2025
Department of Microbiology, Immunology, and Tropical Medicine, The George Washington University School of Medicine and Health Sciences, Washington, DC, USA.
Trained immunity (TRIM) is a form of long-lasting functional reprogramming of innate immune cells and their progenitors that enhances responsiveness to subsequent stimuli. Although first characterized in myeloid cells, TRIM was recently extended to nonmyeloid cell types, including endothelial and glial cells, which also exhibit stimulus-driven, memory-like behavior. While initially recognized as a protective mechanism, particularly in the context of vaccines and acute infections, TRIM can also become maladaptive, promoting chronic inflammation, immune dysfunction, and disease.
View Article and Find Full Text PDFJ Infect Dis
September 2025
Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, MP, India.
Chandipura virus (CHPV), a Rhabdoviridae family member, is an emerging neurotropic pathogen responsible for acute encephalitis outbreaks in children, mainly in India. Despite its public health relevance, the mechanisms underlying CHPV entry into host cells remain poorly understood. In this study, we used pharmacological inhibitors in Vero cells to dissect the virus's entry pathways.
View Article and Find Full Text PDFJ Neuroinflammation
August 2025
Scientific Research Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, 518107, China.
Unlabelled: Alzheimer’s disease (AD) is the most common type of dementia. A major pathological feature of AD is the aggregation of amyloid-β (Aβ), primarily driven by β-secretase (BACE1) activity. However, the mechanisms underlying continuous Aβ accumulation remain unclear.
View Article and Find Full Text PDF