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Noriko Oshiro

Researcher at Kobe University

Publications -  36
Citations -  8587

Noriko Oshiro is an academic researcher from Kobe University. The author has contributed to research in topics: Phosphorylation & P70-S6 Kinase 1. The author has an hindex of 29, co-authored 36 publications receiving 7990 citations. Previous affiliations of Noriko Oshiro include Nara Institute of Science and Technology & Harvard University.

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Journal ArticleDOI

Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy

TL;DR: A novel mammalian autophagy factor, Atg13, is reported, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200, and suggests that mTORC1 suppressesAutophagy through direct regulation of the approximately 3,MDa ULK 1-Atg13-FIP200 complex.
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Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action.

TL;DR: Raptor is an essential scaffold for the mTOR-catalyzed phosphorylation of 4EBP1 and mediates TOR action in vivo and yields an array of phenotypes that closely resemble those produced by inactivation of Ce-TOR.
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The Mammalian Target of Rapamycin (mTOR) Partner, Raptor, Binds the mTOR Substrates p70 S6 Kinase and 4E-BP1 through Their TOR Signaling (TOS) Motif

TL;DR: Raptor appears to serve as an mTOR scaffold protein, the binding of which to the TOS motif of mTOR substrates is necessary for effective mTOR-catalyzed phosphorylation in vivo and perhaps for conferring their sensitivity to rapamycin and amino acid sufficiency.
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mTOR is essential for growth and proliferation in early mouse embryos and embryonic stem cells.

TL;DR: Deletion of the C-terminal six amino acids of mTOR, which are essential for kinase activity, resulted in reduced cell size and proliferation arrest in embryonic stem cells, and showed that mTOR controls both cell Size and proliferation in early mouse embryos and embryonicstem cells.
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Phosphorylation of Myosin-Binding Subunit (Mbs) of Myosin Phosphatase by Rho-Kinase in Vivo

TL;DR: Results indicate that MBS is phosphorylated by Rho-kinase downstream of Rho in vivo, and suggest that myosin phosphatase and Rho -kinase spatiotemporally regulate the phosphorylation state of RHo-kinases substrates including MLC and ERM family proteins in vivo in a cooperative manner.