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Masanao Kinoshita Last modified date:2021.06.21

Assistant Professor / Bioanalitical Chemistry
Department of Chemistry
Faculty of Sciences


Graduate School


Homepage
https://kyushu-u.pure.elsevier.com/en/persons/masanao-kinoshita
 Reseacher Profiling Tool Kyushu University Pure
Academic Degree
Science
Country of degree conferring institution (Overseas)
Yes
Field of Specialization
Biophysics
Total Priod of education and research career in the foreign country
00years00months
Research
Research Interests
  • membrane structures and properties
    keyword : lipid rafts
    2019.06~2019.06.
  • membrane sructures, properties and dynamics
    keyword : membrane sructures, properties, dynamics
    2015.10~2015.10.
Academic Activities
Papers
1. Masanao Kinoshita, Kenichi G. N. Suzuki, Nobuaki Matsumori, Misa Takada, Hikaru Ano, Kenichi Morigaki, Mitsuhiro Abe, Asami Makino, Toshihide Kobayashi, Koichiro M. Hirosawa, Takahiro K. Fujiwara, Akihiro Kusumi, Michio Murata, Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs, JOURNAL OF CELL BIOLOGY, 10.1083/jcb.201607086, 216, 4, 1183-1204, 2017.04, 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 similar to 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..