Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs
抄録
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–dependent manners, and that, for ∼10–50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size–, cholesterol-, and GPI anchoring–dependent manners. These results suggest that SM continually and rapidly exchanges between CD59-associated raft domains and the bulk PM.
収録刊行物
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- The Journal of Cell Biology
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The Journal of Cell Biology 216 (4), 1183-1204, 2017-03-22
Rockefeller University Press
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詳細情報 詳細情報について
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- CRID
- 1050001202607069312
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- NII論文ID
- 120005998045
- 120006409114
- 120006363304
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- ISSN
- 00219525
- 15408140
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- HANDLE
- 2433/219127
- 20.500.14094/90004352
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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