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Hiroyuki Kumeta on Muck Rack

Hiroyuki Kumeta

As seen in: Nature, MDPI, ACS Publications, BioRxiv, The Journal of Biological Chemistry
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Articles

Transient dynamics of flavonoid metabolons tune chalcone synthase specificity

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By Riki Imaizumi, Toshiyuki Waki, Yoshikazu Hattori, Kohei Takeshita, Miru Sumita, Kazutomo Kawaguchi, Hiroyuki Kumeta, Kenichi Umeda, Kyohei Sato, Taro Yanai, Hiroaki Matsuura, Takeshi Yokoyama, Risa Omura, Kayo Nakatani, Naoki Sakai, Yukimura Kawagiwa, Yamato Doi, Aoi Yasuda, Takuya Nakano, Kaichi Uno, Kunihiro Yoshida, Misato Tsunashima, Tomohide Saio, Yoshikazu Tanaka, Seiji Takahashi, Noriyuki Kodera, Kunishige Kataoka, Masaki Yamamoto, Satoshi Yamashita, Toru Nakayama
| Nature Verified
Abstract Cells achieve metabolic precision by assembling enzymes into dynamic complexes, but the regulatory mechanism of these metabolons is unclear. Here we characterize the chalcone synthase (CHS)–chalcone isomerase-like protein (CHIL) complex, a key component of flavonoid metabolons. While crystallography provides a static view, our analyses reveal that CHS undergoes rapid, reversible binding cycles with CHIL that regulate catalysis in real time.
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A system of paired polyether epoxide hydrolases enables a mouldable enzyme for consecutive ring cyclization cascades

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By Atsushi Minami, Taro Ozaki, Shusuke Sato, Aoi Sugiyama, Takashi Tadokoro, Tomoyasu Aizawa, Tomo Nomai, Takanori Matsumaru, Junyang Liu, Tao Ye, Susumu Uchiyama, Kowit Hengphasatporn, Yasuteru Shigeta, Tomohide Saio, Katsumi Maenaka, Min Yao, Hiroyuki Kumeta, Hideaki Oikawa, Toyoyuki Ose, Nana Yabuno, Yuki Owada, Kohei Sawada, Ayaka Arai, Takuya Dosen, Atsuji Kodama
| Nature Verified
Abstract Ionophore polyethers, a major class of polyketide-derived natural products, are characterized by molecular skeletons featuring arrays of tetrahydrofuran and tetrahydropyran rings. However, the precise mechanism underlying their biosynthesis, suggested to occur by a sequential epoxide-opening and ether cyclization cascade to generate more than two ether rings, remains elusive.
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Ca2+-driven PDIA6 biomolecular condensation ensures proinsulin folding - Nature Cell Biology

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By Young-Ho Lee, Tomohide Saio, Motonori Matsusaki, Shingo Kanemura, Taro Mannen, Michiko Tajiri, Shuichiro Oshita, Yoshikazu Hattori, Hiroyuki Kumeta, Hiroya Abe, Eiichiro Mori, Takahiro Muraoka, Takakazu Nakabayashi, Michele Vendruscolo
| Nature Verified
Abstract The endoplasmic reticulum (ER) plays crucial roles in maintaining protein quality control and regulating dynamic Ca2+ storage in eukaryotic cells. However, the proteostasis system involved in ER-mediated protein quality control has not been fully characterized. Here we show that Ca2+ triggers the condensation of PDIA6, an ER-resident disulfide isomerase and molecular chaperone, into quality control granules.
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