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  2. 金井 好克

金井 好克

カナイ ヨシカツ  (Yoshikatsu Kanai)

基本情報

所属
藤田医科大学 研究推進本部　産官学連携推進センター 特命教授
大阪大学 ヒューマン・メタバース疾患研究拠点（WPI-PRIMe） 特任教授
学位
医学士(1984年3月)
医学博士(1988年3月)
研究者番号
60204533
J-GLOBAL ID
200901003262194571
researchmap会員ID
1000305140
外部リンク

研究キーワード

 6

研究分野

 4

経歴

 10
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学歴

 2

受賞

 12
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論文

 464
  • Shinichi Sakamoto, Yukio Naya, Junryo Rii, Kazumi Taguchi, Masaaki Fujimura, Yasuhiro Shigeta, Arthit Chairoungdua, Motoi Nishimura, Ken Wakai, Yasutaka Yamada, Xue Zhao, Yusuke Imamura, Sawako Tajima, Natsumi Sato, Chiaki Hosaka, Mizuka Sekine, Takeshi Ueda, Shuzo Hamamoto, Takahiro Yasui, Yoshikatsu Kanai, Koichiro Akakura, Yuzuru Ikehara, Naohiko Anzai, Tomohiko Ichikawa
    Scientific Reports 15(1) 2025年9月26日  査読有り
  • Anzu Nishiwaki, Hiroki Okanishi, Yoshikatsu Kanai, Ryoji Masui
    FEBS Open Bio 2025年9月15日  査読有り
    In Thermus thermophilus, an aerobic Gram‐negative eubacterium used as a model organism, more than half of the phosphorylation sites identified by proteomic analysis are located near the ligand‐binding site, including the active site, of the enzyme in the three‐dimensional structure. We investigated the effect of these phosphorylation events on the activity of six enzymes (three nucleoside monophosphate kinases, isocitrate kinase, malate dehydrogenase and inorganic pyrophosphatase) by introducing phosphomimetic mutations, Glu, into the phosphorylation sites. All phosphomimetic mutants showed severely reduced activity compared with the wild‐type, particularly in the turnover number. The proteins analyzed in this study belong to different families and have various functions. This suggests that there is a widespread mechanism by which phosphorylation of amino acid residues near the active site reduces enzyme activity independent of the protein family and function.
  • Yongchan Lee, Chunhuan Jin, Ryuichi Ohgaki, Minhui Xu, Satoshi Ogasawara, Rangana Warshamanage, Keitaro Yamashita, Garib Murshudov, Osamu Nureki, Takeshi Murata, Yoshikatsu Kanai
    Nature Communications 16(1) 2025年2月14日  査読有り最終著者責任著者
    Abstract LAT1 (SLC7A5) transports large neutral amino acids and plays pivotal roles in cancer proliferation, immune response and drug delivery. Despite recent advances in structural understanding of LAT1, how it discriminates substrates and inhibitors including the clinically relevant drugs remains elusive. Here we report six structures of LAT1 across three conformations with bound ligands, elucidating its substrate transport and inhibitory mechanisms. JPH203 (also known as nanvuranlat or KYT-0353), an anticancer drug in clinical trials, traps LAT1 in an outward-facing state with a U-shaped conformer, with its amino-phenylbenzoxazol moiety pushing against transmembrane helix 3 (TM3) and bending TM10. Physiological substrates like ʟ-Phe lack such effects, whereas melphalan poses steric hindrance, explaining its inhibitory activity. The “classical” system L inhibitor BCH induces an occluded state critical for transport, confirming its substrate-like behavior. These findings provide a structural basis for substrate recognition and inhibition of LAT1, guiding future drug design.
  • Yunlong Sui, Namiko Hoshi, Norihiro Okamoto, Yuta Inoue, Takumi Funatsu, Yuna Ku, Makoto Ooi, Daisuke Watanabe, Haruka Miyazaki, Misaki Agawa, Hirotaka Nakamura, Ryuichi Ohgaki, Yoshikatsu Kanai, Hui Yang, Yuzo Kodama
    Biochemical and Biophysical Research Communications 151446-151446 2025年2月  査読有り
  • Chunhuan Jin, Xinyu Zhou, Minhui Xu, Hiroki Okanishi, Ryuichi Ohgaki, Yoshikatsu Kanai
    Scientific Reports 15(1) 2025年1月23日  査読有り最終著者責任著者
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MISC

 431

書籍等出版物

 41
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講演・口頭発表等

 38
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所属学協会

 16
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共同研究・競争的資金等の研究課題

 51
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産業財産権

 68
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