T
Takuya Saiwaki
Researcher at Osaka University
Publications - 9
Citations - 619
Takuya Saiwaki is an academic researcher from Osaka University. The author has contributed to research in topics: Importin & Nuclear transport. The author has an hindex of 8, co-authored 9 publications receiving 570 citations. Previous affiliations of Takuya Saiwaki include Heidelberg University.
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Journal ArticleDOI
Cellular stresses induce the nuclear accumulation of importin α and cause a conventional nuclear import block
Yoichi Miyamoto,Takuya Saiwaki,Junichi Yamashita,Yoshinari Yasuda,Ippei Kotera,Satoshi Shibata,Masaki Shigeta,Yasushi Hiraoka,Yasushi Hiraoka,Tokuko Haraguchi,Tokuko Haraguchi,Yoshihiro Yoneda +11 more
TL;DR: It is reported here that importin α accumulates reversibly in the nucleus in response to cellular stresses including UV irradiation, oxidative stress, and heat shock, and the findings suggest that the stress-induced nuclear accumulation of importinα can be involved in a common physiological response to various stress conditions.
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Importin α can migrate into the nucleus in an importin β‐ and Ran‐independent manner
Yoichi Miyamoto,Miki Hieda,Michelle T. Harreman,Masahiro Fukumoto,Takuya Saiwaki,Alec E. Hodel,Anita H. Corbett,Yoshihiro Yoneda +7 more
TL;DR: It is found that importin α migrated into the nucleus without the addition of importin β, Ran or any other soluble factors in an in vitro transport assay, suggesting that the nuclear import machinery for importinα at individual nuclear pore complexes may be regulated by reaction(s) that require ATP hydrolysis.
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Importin α transports CaMKIV to the nucleus without utilizing importin β
Ippei Kotera,Toshihiro Sekimoto,Yoichi Miyamoto,Takuya Saiwaki,Emi Nagoshi,Hiroyuki Sakagami,Hisatake Kondo,Yoshihiro Yoneda +7 more
TL;DR: It is reported here that importin α is able to carry CaMKIV into the nucleus without the need for importin β or any other soluble proteins in digitonin‐permeabilized cells.
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A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis.
TL;DR: The identification of a putative RNA-binding protein of 293 residues as another binding partner of the FHA domain of pKi-67 (referred to as NIFK for nucleolar proteininteracting with the F HA) is reported on, suggesting that hNIFK interacts with Ki-FHA in a mitosis-specific and phosphorylation-dependent manner.
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Mechanism of the stress-induced collapse of the Ran distribution
TL;DR: It is reported here that a decrease in stress-induced ATP is associated with an increase in cytoplasmic Ran levels and a collapse of Ran distribution, and this indicates that the decrease in ATP levels induced by cellular stress causes a decreases in RanGTP levels andA collapse in Ran distribution.