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Atsushi Kosugi

Researcher at Osaka University

Publications -  44
Citations -  3267

Atsushi Kosugi is an academic researcher from Osaka University. The author has contributed to research in topics: T cell & Antigen. The author has an hindex of 23, co-authored 44 publications receiving 3137 citations.

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Journal ArticleDOI

Essential role of MD-2 in LPS responsiveness and TLR4 distribution.

TL;DR: It is found that in MD-2−/− embryonic fibroblasts, TLR4 was not able to reach the plasma membrane and predominantly resided in the Golgi apparatus, whereas TLR3 was distributed at the leading edge surface of cells in wild-type embryonic fibrablasts andMD-2 is essential for correct intracellular distribution and LPS-recognition ofTLR4.
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Lipopolysaccharide Interaction with Cell Surface Toll-like Receptor 4-MD-2 Higher Affinity than That with MD-2 or CD14

TL;DR: Direct LPS interaction with cell surface TLR4-MD-2 that is distinct from that with MD-2 or CD14 is revealed, suggesting a role for CD14 in LPS loading onto TLR2 but not in the interaction itself between LPS and TLR3-MD2.
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Essential role for ERK2 mitogen-activated protein kinase in placental development.

TL;DR: This data indicates that suppression of ERK2 in response to EMT has an important role in cell proliferation, differentiation, and survival and its role in vivo remains to be determined.
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Lipid A antagonist, lipid IVa, is distinct from lipid A in interaction with Toll-like receptor 4 (TLR4)-MD-2 and ligand-induced TLR4 oligomerization.

TL;DR: L ligand-induced TLR4 oligomerization, homotypic interaction ofTLR4, which directly leads to TLR3 signaling, and MD-2 has an important role in a link between ligand interaction and TLR 4 oligomerized.
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Cutting edge: Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells.

TL;DR: A negative regulatory role for Fyn is elucidated in proximal TCR signaling in lipid rafts after it was demonstrated that Fyn, but not Lck, has its kinase activity in membrane rafts, and plays a critical role in Cbp phosphorylation, Cbp-Csk interaction, and Csk Kinase activity.