R
Ryuichi Sakai
Researcher at Kitasato University
Publications - 84
Citations - 6111
Ryuichi Sakai is an academic researcher from Kitasato University. The author has contributed to research in topics: Phosphorylation & Tyrosine phosphorylation. The author has an hindex of 37, co-authored 76 publications receiving 5725 citations. Previous affiliations of Ryuichi Sakai include National Cancer Research Institute & Mount Sinai Hospital, Toronto.
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Journal ArticleDOI
Force Sensing by Mechanical Extension of the Src Family Kinase Substrate p130Cas
Yasuhiro Sawada,Masako Tamada,Benjamin J. Dubin-Thaler,Oksana Cherniavskaya,Ryuichi Sakai,Sakae Tanaka,Michael P. Sheetz +6 more
TL;DR: This work mechanically extended bacterially expressed Cas substrate domain protein (CasSD) in vitro and found a remarkable enhancement of phosphorylation by Src family kinases with no apparent change in kinase activity.
Journal ArticleDOI
A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner.
Ryuichi Sakai,Akihiro Iwamatsu,Naoto Hirano,Seishi Ogawa,Tomoyuki Tanaka,Hiroyuki Mano,Yoshio Yazaki,H Hirai +7 more
TL;DR: The p130 (designated Cas for Crk‐associated substrate) is a common cellular target of phosphorylation signal via v‐Crk and v‐Src oncoproteins, and its unique structure indicates the possible role of p130Cas in assembling signals from multiple SH2‐containing molecules.
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Mammalian grb2 regulates multiple steps in embryonic development and malignant transformation
Alec M. Cheng,Tracy M. Saxton,Tracy M. Saxton,Ryuichi Sakai,Sarang Kulkarni,Geraldine Mbamalu,Wolfgang F. Vogel,Christopher G. Tortorice,Robert D. Cardiff,James C. Cross,James C. Cross,William J. Muller,Tony Pawson,Tony Pawson +13 more
TL;DR: Analysis of mutant embryonic stem cells, embryos, and chimeras reveals that Grb2 is required during embyrogenesis for the differentiation of endodermal cells and formation of the epiblast and is rate limiting for mammary carcinomas induced by polyomavirus middle T antigen.
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Integrin-mediated Cell Adhesion Promotes Tyrosine Phosphorylation of p130Cas, a Src Homology 3-containing Molecule Having Multiple Src Homology 2-binding Motifs
Yoshihisa Nojima,Noritsugu Morino,Toshihide Mimura,Ken Hamasaki,Hiroko Furuya,Ryuichi Sakai,Toshiya Sato,Kouichi Tachibana,Chikao Morimoto,Yoshio Yazaki,Hisamaru Hirai +10 more
TL;DR: It is proposed that Cas may amplify and propagate integrin-mediated signals by interacting with SH2-containing molecule(s) and play a role in signaling pathways mediated by cell adhesion as well as by transformation.
Journal ArticleDOI
Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases.
TL;DR: There is an excellent correlation between the ability of mutant Crk proteins to promote hyperphosphorylation of p130 by Abl and their ability to transform rodent fibroblasts and the substrate specificity of a non-receptor tyrosine kinase is dependent on the binding specificity of its associated SH2 domain.