Summary of ssbd-repos-000110

SSBD:database
URL

Name
ssbd-repos-000110 (110-Makino-MembraneDyn)
URL
DOI
-

Title
Immunoelectron microscopic images of nakanori distribution in HeLa cells, human skin fibroblasts and NPC cells
Description
-
Submited Date
-
Release Date
2018-11-14
Updated Date
-
License
Funding information
-
File formats
Data size
60.2 MB

Organism
H. sapiens
Strain
fibroblast, HeLa , NPC
Cell Line
-
Genes
-
Proteins
-

GO Molecular Function (MF)
-
GO Biological Process (BP)
protein lipid complex assembly
GO Cellular Component (CC)
plasma membrane, protein lipid complex
Study Type
-
Imaging Methods
-

Method Summary
-
Related paper(s)

Asami Makino, Mitsuhiro Abe, Reiko Ishitsuka, Motohide Murate, Takuma Kishimoto, Shota Sakai, Francoise Hullin-Matsuda, Yukiko Shimada, Takehiko Inaba, Hideyuki Miyatake, Hideko Tanaka, Atsushi Kurahashi, Chan-Gi Pack, Rinshi S Kasai, Shuku Kubo, Nicole L Schieber, Naoshi Dohmae, Naoya Tochio, Kyoji Hagiwara, Yutaka Sasaki, Yoko Aida, Fumihiro Fujimori, Takanori Kigawa, Kozo Nishibori, Robert G Parton, Akihiro Kusumi, Yasushi Sako, Gregor Anderluh, Makoto Yamashita, Tetsuyuki Kobayashi, Peter Greimel, Toshihide Kobayashi (2017) A novel sphingomyelin/cholesterol domain-specific probe reveals the dynamics of the membrane domains during virus release and in Niemann-Pick type C., FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Volume 31, Number 4, pp. 1301-1322

Published in 2017 Apr (Electronic publication in Aug. 4, 2016, midnight )

(Abstract) We identified a novel, nontoxic mushroom protein that specifically binds to a complex of sphingomyelin (SM), a major sphingolipid in mammalian cells, and cholesterol (Chol). The purified protein, termed nakanori, labeled cell surface domains in an SM- and Chol-dependent manner and decorated specific lipid domains that colocalized with inner leaflet small GTPase H-Ras, but not K-Ras. The use of nakanori as a lipid-domain-specific probe revealed altered distribution and dynamics of SM/Chol on the cell surface of Niemann-Pick type C fibroblasts, possibly explaining some of the disease phenotype. In addition, that nakanori treatment of epithelial cells after influenza virus infection potently inhibited virus release demonstrates the therapeutic value of targeting specific lipid domains for anti-viral treatment.-Makino, A., Abe, M., Ishitsuka, R., Murate, M., Kishimoto, T., Sakai, S., Hullin-Matsuda, F., Shimada, Y., Inaba, T., Miyatake, H., Tanaka, H., Kurahashi, A., Pack, C.-G., Kasai, R. S., Kubo, S., Schieber, N. L., Dohmae, N., Tochio, N., Hagiwara, K., Sasaki, Y., Aida, Y., Fujimori, F., Kigawa, T., Nishibori, K., Parton, R. G., Kusumi, A., Sako, Y., Anderluh, G., Yamashita, M., Kobayashi, T., Greimel, P., Kobayashi, T. A novel sphingomyelin/cholesterol domain-specific probe reveals the dynamics of the membrane domains during virus release and in Niemann-Pick type C.
(MeSH Terms)

Contact(s)
Toshihide Kobayashi
Organization(s)
University of Strasbourg , Faculty of pharmacy , UMR 7021 CNRS
Image Data Contributors
Quantitative Data Contributors

Download files
Download zipped files