K
Ken-ichi Yoshino
Researcher at Kobe University
Publications - 78
Citations - 5943
Ken-ichi Yoshino is an academic researcher from Kobe University. The author has contributed to research in topics: Mass spectrometry & Phosphorylation. The author has an hindex of 29, co-authored 72 publications receiving 5630 citations. Previous affiliations of Ken-ichi Yoshino include Hochschule Hannover & Osaka University.
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Journal ArticleDOI
Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action.
Kenta Hara,Yoshiko Maruki,Xiaomeng Long,Ken-ichi Yoshino,Noriko Oshiro,Sujuti Hidayat,Chiharu Tokunaga,Joseph Avruch,Kazuyoshi Yonezawa +8 more
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.
Journal ArticleDOI
The Mammalian Target of Rapamycin (mTOR) Partner, Raptor, Binds the mTOR Substrates p70 S6 Kinase and 4E-BP1 through Their TOR Signaling (TOS) Motif
Hiroki Nojima,Hiroki Nojima,Chiharu Tokunaga,Satoshi Eguchi,Noriko Oshiro,Sujuti Hidayat,Ken-ichi Yoshino,Kenta Hara,Noriaki Tanaka,Joseph Avruch,Kazuyoshi Yonezawa +10 more
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.
Journal ArticleDOI
Tor directly controls the Atg1 kinase complex to regulate autophagy.
Yoshiaki Kamada,Ken-ichi Yoshino,Chika Kondo,Tomoko Kawamata,Noriko Oshiro,Kazuyoshi Yonezawa,Yoshinori Ohsumi +6 more
TL;DR: It is suggested that the direct control of the Atg1 complex by TORC1 induces autophagy, and expression of an unphosphorylatable Atg13 mutant bypasses theTORC1 pathway to induce autophagic through activation of Atg2 in cells growing under nutrient-rich conditions.
Journal ArticleDOI
A possible linkage between AMP‐activated protein kinase (AMPK) and mammalian target of rapamycin (mTOR) signalling pathway
Naoki Kimura,Chiharu Tokunaga,Sushila R. Dalal,Christine A. Richardson,Ken-ichi Yoshino,Kenta Hara,Bruce E. Kemp,Lee A. Witters,Osamu Mimura,Kazuyoshi Yonezawa +9 more
TL;DR: The mammalian target of rapamycin (mTOR) regulates multiple cellular functions including translation in response to nutrients, especially amino acids, and AMP‐activated protein kinase (AMPK) modulates metabolism in Response to energy demand by responding to changes in AMP.
Journal ArticleDOI
The Proline-rich Akt Substrate of 40 kDa (PRAS40) Is a Physiological Substrate of Mammalian Target of Rapamycin Complex 1
Noriko Oshiro,Rinako Takahashi,Ken-ichi Yoshino,Keiko Tanimura,Akio Nakashima,Satoshi Eguchi,Takafumi Miyamoto,Kenta Hara,Kenji Takehana,Joseph Avruch,Ushio Kikkawa,Kazuyoshi Yonezawa +11 more
TL;DR: RNA interference-induced depletion of PRAS40 enhanced the amino acid-stimulated phosphorylation of both S6K1 and 4E-BP1 and indicates that the ability of raptor to bind endogenous substrates is limiting for the activity of mTORC1 in vivo and is therefore a potential locus of regulation.