Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
Tracking the localization and dynamics of the intracellular bioactive lipid phosphatidic acid (PA) is important for understanding diverse biological phenomena. Although several PA sensors have been developed, better ones are still needed for comprehensive PA detection in cells. We recently found that α-synuclein (α-Syn) selectively and strongly bound to PA in vitro. Here, we revealed that the N-terminal region of α-Syn (α-Syn-N) specifically bound to PA, with a dissociation constant of 6.6 μm. α-Syn-N colocalized with PA-producing enzymes, diacylglycerol kinase (DGK) β at the plasma membrane (PM), myristoylated DGKζ at the Golgi apparatus, phorbol ester-stimulated DGKγ at the PM, and phospholipase D2 at the PM and Golgi but not with the phosphatidylinositol-4,5-bisphosphate-producing enzyme in COS-7 cells. However, α-Syn-N failed to colocalize with them in the presence of their inhibitors and/or their inactive mutants. These results indicate that α-Syn-N specifically binds to cellular PA and can be applied as an excellent PA sensor.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1111/febs.15137 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Charge-dependent localization of Toll-like receptor 5 at the plasma membrane.
Mol Cells
September 2025
Graduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea. Electronic address:
Proper subcellular localization of Toll-like receptors (TLRs) is essential for initiating appropriate innate immune responses against pathogens while avoiding self-reactivity. UNC93B1 is known to mediate the intracellular trafficking of nucleotide-sensing TLRs such as TLR9 which undergoes rapid internalization into endolysosomes upon reaching the cell surface. We previously demonstrated that UNC93B1 also facilitates the plasma membrane localization of TLR5, a sensor for bacterial flagellin.
View Article and Find Full Text PDFCowpea Lipid Transfer Protein LTP1 Mediates Plant Resistance to .
Mol Plant Microbe Interact
September 2025
Huazhong Agricultural University, College of Life Science and Technology, Wuhan, Hubei , China;
Plant lipid transfer proteins (LTPs), belonging to pathogenesis-related protein 14 family, participate in plant immune response to biotic stress. LTP1 from was previously shown to be able to suppress infection by cowpea mosaic virus and soybean mosaic virus. However, whether cowpea LTP1 participates in the plant resistance to other plant pathogens remains unclear.
View Article and Find Full Text PDFGlycosylphosphatidylinositol biosynthesis functions as a conserved host defense pathway against coronaviruses via regulation of LY6E.
PLoS Pathog
September 2025
Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Shanghai Medical College, Fudan University, Shanghai, China.
Coronaviruses, including SARS-CoV-2, rely on host factors for their replication and pathogenesis, while hosts deploy defense mechanisms to counteract viral infections. Although numerous host proviral factors have been identified, the landscape of host restriction factors and their underlying mechanisms remain less explored. Here, we conducted genome-wide CRISPR knockout screens using three distinct coronaviruses-SARS-CoV-2, HCoV-OC43 (a common cold human virus from the genus Betacoronavirus) and porcine epidemic diarrhea virus (Alphacoronavirus) to identify conserved host restriction factors.
View Article and Find Full Text PDFMultiple interactions recruit BLTP2 to ER-PM contacts to control plasma membrane dynamics.
J Cell Biol
September 2025
Department of Neuroscience, Yale University School of Medicine, New Haven, CT, USA.
BLTP2/KIAA0100, a bridge-like lipid transfer protein, was reported to localize at contacts of the ER with either the plasma membrane (PM) or recycling tubular endosomes depending on the cell type. Our findings suggest that mediating bulk lipid transport between the ER and the PM is a key function of this protein, as BLTP2 tethers the ER to tubular endosomes only after they become continuous with the PM and that it also tethers the ER to macropinosomes in the process of fusing with the PM. We further identify interactions underlying binding of BLTP2 to the PM, including phosphoinositides, the adaptor proteins FAM102A/FAM102B, and N-BAR domain proteins at membrane-connected tubules.
View Article and Find Full Text PDFReelin Increases the Sphingomyelin Content of the Plasma Membrane and Affects the Surface Expression of GPI-Anchored Proteins in Hippocampal Neurons.
J Neurochem
September 2025
Department of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, Japan.
Sphingomyelin (SM) is primarily located in the outer leaflet of the plasma membrane. It plays a crucial role in intercellular communication and the morphology of neuronal cells by influencing the localization and function of various proteins. However, the mechanisms regulating the SM content in the neuronal plasma membrane remain largely elusive.
View Article and Find Full Text PDF