Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs
| Autor: | Takahiro K. Fujiwara, Kenichi G. N. Suzuki, Masanao Kinoshita, Mitsuhiro Abe, Misa Takada, Toshihide Kobayashi, Nobuaki Matsumori, Kenichi Morigaki, Michio Murata, Akihiro Kusumi, Koichiro M. Hirosawa, Hikaru Ano, Asami Makino |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Fluorophore Glycosylphosphatidylinositols Swine Detergents CD59 Antigens CHO Cells Biology Cell Line Tools 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Cricetulus Membrane Microdomains Animals Research Articles Fluorescent Dyes Sphingolipids Sphingosine Cell Membrane Cell Biology Raft Fluorescence Sphingolipid Sphingomyelins carbohydrates (lipids) 030104 developmental biology Membrane Cholesterol Biochemistry chemistry Biophysics lipids (amino acids peptides and proteins) Sphingomyelin Linker Hydrophobic and Hydrophilic Interactions 030217 neurology & neurosurgery |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 0021-9525 |
| Popis: | Sphingomyelin (SM) has been proposed to form cholesterol-dependent raft domains and sphingolipid domains in the plasma membrane (PM). How SM contributes to the formation and function of these domains remains unknown, primarily because of the scarcity of suitable fluorescent SM analogs. We developed new fluorescent SM analogs by conjugating a hydrophilic fluorophore to the SM choline headgroup without eliminating its positive charge, via a hydrophilic nonaethylene glycol linker. The new analogs behaved similarly to the native SM in terms of their partitioning behaviors in artificial liquid order-disorder phase-separated membranes and detergent-resistant PM preparations. Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone{textendash}dependent manners, and that, for ~{}10{textendash}50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size{textendash}, cholesterol-, and GPI anchoring{textendash}dependent manners. These results suggest that SM continually and rapidly exchanges between CD59-associated raft domains and the bulk PM. 脂質の挙動をありのままに再現する蛍光プローブでラフトの形成機構を解明. 京都大学プレスリリース. 2017-03-28. |
| Databáze: | OpenAIRE |
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