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Lipid-protein interactions play essential roles in cellular signaling and membrane dynamics, yet their systematic characterization has long been hindered by the inherent biochemical properties of lipids. Recent advances in functionalized lipid probes - equipped with photoactivatable crosslinkers, affinity handles, and photocleavable protecting groups - have enabled proteomics-based identification of lipid interacting proteins with unprecedented specificity and resolution. Despite the growing number of published lipid interactomes, there remains no centralized effort to harmonize, compare, or integrate these datasets. The Lipid Interactome addresses this gap by providing a structured, interactive web portal that adheres to FAIR data principles - ensuring that lipid interactome studies are Findable, Accessible, Interoperable, and Reusable. Through standardized data formatting, interactive visualizations, and direct cross-study comparisons, this resource enables researchers to systematically explore the protein-binding partners of diverse bioactive lipids. By consolidating and curating lipid interactome proteomics data from multiple studies, the Lipid Interactome database serves as a critical tool for deciphering the biological functions of lipids in cellular systems.
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Plant Physiol Biochem
September 2025
Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada. Electronic address:
Many plant-derived unusual fatty acids (UFAs) possess valuable chemical properties and have potential applications in the food, feed, and oleochemical industries. Despite significant interest, the mechanisms by which plants synthesize and accumulate these structurally distinct fatty acids remain only partially understood. While enzyme substrate specificities involved in UFA-containing storage lipid assembly have been well characterized in many prior studies, the biochemical roles of protein-protein interactions (PPIs) in coordinating UFA biosynthesis have received less attention.
View Article and Find Full Text PDFData 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 PDFRes Sq
August 2025
Cleveland Clinic Genome Center, Cleveland Clinic Research, Cleveland Clinic, Cleveland, OH 44195, USA.
Alzheimer's disease (AD) exhibits metabolic heterogeneity; yet, the consequences on metabolic dynamics in a cell-type-specific manner and the underlying metabolite-sensor network basis remain unclear. Here, we show that neurons exhibit a striking decrease in energy and lipid-related metabolic activity, contrasted by an increase in microglial metabolism associated with neuroinflammation. To identify brain cell-type specific master metabolic regulators underlying the metabolic alterations of AD, we introduce scFUMES (ingle ell nctional tabolite-ensor), an algorithm integrating single-cell RNA sequencing, interactomics (protein-protein interactions), genomics, transcriptomics, and metabolomics from large human brain biobanks.
View Article and Find Full Text PDFPlant Physiol Biochem
August 2025
Department of Biotechnology, Thapar Institute of Engineering and Technology Patiala, Punjab, India. Electronic address:
Plant membrane transporters are essential for perceiving salinity stress, transducing signals, and mitigating stress during salt exposure. These proteins reside in the membrane and are modulated by various cellular components, including membrane lipids. Certain specific lipids are known to modulate the activity of plant membrane transporters, influencing their structure, function, and distribution within the membrane.
View Article and Find Full Text PDFInt J Mol Sci
August 2025
The Helen B Taussig Heart Center, Cardiovascular Innovation Laboratory, Division of Cardiology, Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA.
UDP-Gal-β-1,4 galactosyltransferase-V (GalT-V) is a member of a large family of galactosyltransferases whose function is to transfer galactose from the nucleotide sugar UDP-galactose to a glycosphingolipid glucosylceramide, to generate lactosylceramide (LacCer). It also causes the N and O glycosylation of proteins in the Trans Golgi area. LacCer is a bioactive lipid second messenger that activates an "oxidative stress pathway", leading to critical phenotypes, e.
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