T
Toshimasa Ishizaki
Researcher at Oita University
Publications - 74
Citations - 15854
Toshimasa Ishizaki is an academic researcher from Oita University. The author has contributed to research in topics: MDia1 & Actin cytoskeleton. The author has an hindex of 42, co-authored 68 publications receiving 15248 citations. Previous affiliations of Toshimasa Ishizaki include Max Planck Society & Kyoto University.
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Journal ArticleDOI
Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension
Masayoshi Uehata,Toshimasa Ishizaki,Hiroyuki Satoh,Takashi Ono,Toshio Kawahara,Tamami Morishita,Hiroki Tamakawa,Keiji Yamagami,Jun Inui,Midori Maekawa,Shuh Narumiya +10 more
TL;DR: Pyridine derivative Y-27632 consistently suppresses Rho-induced, p160ROCK-mediated formation of stress fibres in cultured cells and dramatically corrects hypertension in several hypertensive rat models, suggesting that compounds that inhibit this process might be useful therapeutically.
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Focal Contacts as Mechanosensors Externally Applied Local Mechanical Force Induces Growth of Focal Contacts by an Mdia1-Dependent and Rock-Independent Mechanism
Daniel Riveline,Daniel Riveline,Eli Zamir,Nathalie Q. Balaban,Ulrich S. Schwarz,Toshimasa Ishizaki,Shuh Narumiya,Zvi Kam,Benjamin Geiger,Alexander D. Bershadsky +9 more
TL;DR: Experiments show that integrin-containing focal complexes behave as individual mechanosensors exhibiting directional assembly in response to local force, and that external tension force bypasses the requirement for ROCK-mediated myosin II contractility in the induction of focal contacts.
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Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
TL;DR: It is shown that GTP-bound Rho activates its effector mDia1 by disrupting mDIA1’s intramolecular interactions, which may induce the formation of different actin structures affected by the balance between mDía1 and ROCK signalling.
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The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase.
Toshimasa Ishizaki,Midori Maekawa,Kazuko Fujisawa,Katsuya Okawa,Akihiro Iwamatsu,Akiko Fujita,Naoki Watanabe,Y. Saito,Akira Kakizuka,Narito Morii,Shuh Narumiya +10 more
TL;DR: It is shown that p160 can associate physically and functionally with Rho both in vitro and in vivo, indicating that the small GTP‐binding protein Rho functions as a molecular switch in the formation of focal adhesions and stress fibers, cytokinesis and transcriptional activation.
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p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin.
Naoki Watanabe,Pascal Madaule,Tim Reid,Toshimasa Ishizaki,Go Watanabe,Akira Kakizuka,Y. Saito,Kazuwa Nakao,Brigitte M. Jockusch,Shuh Narumiya +9 more
TL;DR: Results suggest that Rho regulates actin polymerization by targeting profilin via p140mDia beneath the specific plasma membranes.