T
Takanori Ebisawa
Researcher at Japan Society for the Promotion of Science
Publications - 5
Citations - 1624
Takanori Ebisawa is an academic researcher from Japan Society for the Promotion of Science. The author has contributed to research in topics: Phosphorylation & Transforming growth factor beta. The author has an hindex of 5, co-authored 5 publications receiving 1558 citations. Previous affiliations of Takanori Ebisawa include Japanese Foundation for Cancer Research.
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Journal ArticleDOI
Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation.
Takanori Ebisawa,Minoru Fukuchi,Gyo Murakami,Tomoki Chiba,Keiji Tanaka,Takeshi Imamura,Kohei Miyazono,Kohei Miyazono +7 more
TL;DR: It is shown that Smurf1, an E3 ubiquitin ligase for bone morphogenetic protein-specific Smads, also interacts with Smad7 and inducesSmad7 ubiquitination and translocation into the cytoplasm, revealing a novel function of Smad 7, i.e. induction of degradation of TβR-I through recruitment of an E 3 ligase to the receptor.
Journal ArticleDOI
Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation.
Takanori Ebisawa,K. Tada,I. Kitajima,K. Tojo,T.K. Sampath,Masahiro Kawabata,Kohei Miyazono,Takeshi Imamura +7 more
TL;DR: The findings indicate that in the process of differentiation to osteoblasts, BMP-6 binds to ALK-2 as well as other type I receptors, and transduces signals mainly through Smad5 and possibly throughSmad1.
Journal ArticleDOI
Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins.
Minoru Fukuchi,Takeshi Imamura,Tomoki Chiba,Takanori Ebisawa,Masahiro Kawabata,Keiji Tanaka,Kohei Miyazono,Kohei Miyazono +7 more
TL;DR: It is shown that Smad3 activated by TGF-beta is degraded by the ubiquitin-proteasome pathway, and T GF-beta/Smad3 signaling is thus irreversibly terminated by the proteasomal degradation.
Journal ArticleDOI
The N domain of Smad7 is essential for specific inhibition of transforming growth factor-β signaling
Aki Hanyu,Y Ishidou,Takanori Ebisawa,Tomomasa Shimanuki,Takeshi Imamura,Kohei Miyazono,Kohei Miyazono +6 more
TL;DR: Analyses using deletion mutants and chimeras of Smad6 and Smad7 revealed that the MH2 domains were responsible for the inhibition of both TGF-β and BMP signaling by I-Smads, but the isolated MH2 domes were less potent than the full-length Smad 7 in inhibiting T GF-β signaling.
Journal ArticleDOI
Region between α‐helices 3 and 4 of the Mad homology 2 domain of Smad4: functional roles in oligomer formation and transcriptional activation
Keiichiro Tada,Hirofumi Inoue,Takanori Ebisawa,Masatoshi Makuuchi,Masahiro Kawabata,Takeshi Imamura,Kohei Miyazono +6 more
TL;DR: Chimeric constructs of Smad4 containing the region corresponding to the α‐helix 3, H3/4 loop and α-helix 4 of different Smads are prepared, including a chimera containing that ofSmad2 (Smad4‐HL2).