Y
Yoshinobu Ichimura
Researcher at Niigata University
Publications - 49
Citations - 12120
Yoshinobu Ichimura is an academic researcher from Niigata University. The author has contributed to research in topics: Autophagy & ATG8. The author has an hindex of 29, co-authored 46 publications receiving 10415 citations. Previous affiliations of Yoshinobu Ichimura include Juntendo University & Graduate University for Advanced Studies.
Papers
More filters
Journal ArticleDOI
The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
Masaaki Komatsu,Hirofumi Kurokawa,Satoshi Waguri,Keiko Taguchi,Akira Kobayashi,Yoshinobu Ichimura,Yoshinobu Ichimura,Yu-shin Sou,Yu-shin Sou,Izumi Ueno,Ayako Sakamoto,Kit I. Tong,Mihee Kim,Yasumasa Nishito,Shun-ichiro Iemura,Tohru Natsume,Takashi Ueno,Eiki Kominami,Hozumi Motohashi,Keiji Tanaka,Masayuki Yamamoto +20 more
TL;DR: The findings indicate that the pathological process associated with p62 accumulation results in hyperactivation of Nrf2 and delineates unexpected roles of selective autophagy in controlling the transcription of cellular defence enzyme genes.
Journal ArticleDOI
A ubiquitin-like system mediates protein lipidation
Yoshinobu Ichimura,Takayoshi Kirisako,Takayoshi Kirisako,Toshifumi Takao,Yoshinori Satomi,Yasutsugu Shimonishi,Naotada Ishihara,Noboru Mizushima,Noboru Mizushima,Isei Tanida,Eiki Kominami,Mariko Ohsumi,Takeshi Noda,Takeshi Noda,Yoshinori Ohsumi,Yoshinori Ohsumi +15 more
TL;DR: A new mode of protein lipidation is reported, in which Apg8 is covalently conjugated to phosphatidylethanolamine through an amide bond between the C-terminal glycine and the amino group of phosph atidyleanolamine, mediated by a ubiquitination-like system.
Journal ArticleDOI
Atg8, a Ubiquitin-like Protein Required for Autophagosome Formation, Mediates Membrane Tethering and Hemifusion
TL;DR: It is shown using an in vitro system that Atg8 mediates the tethering and hemifusion of membranes, which are evoked by the lipidation of the protein and reversibly modulated by the deconjugation enzyme Atg4.
Journal ArticleDOI
The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy.
Takao Hanada,Nobuo N. Noda,Yoshinori Satomi,Yoshinobu Ichimura,Yuko Fujioka,Toshifumi Takao,Fuyuhiko Inagaki,Yoshinori Ohsumi +7 more
TL;DR: Results indicate that the Atg12-Atg5 conjugate is a ubiquitin-protein ligase (E3)-like enzyme for Atg8-PE conjugation reaction, distinctively promoting protein-lipid conjugations.
Journal ArticleDOI
The Reversible Modification Regulates the Membrane-Binding State of Apg8/Aut7 Essential for Autophagy and the Cytoplasm to Vacuole Targeting Pathway
Takayoshi Kirisako,Yoshinobu Ichimura,Yoshinobu Ichimura,Hisashi Okada,Yukiko Kabeya,Noboru Mizushima,Noboru Mizushima,Tamotsu Yoshimori,Tamotsu Yoshimori,Mariko Ohsumi,Toshifumi Takao,Takeshi Noda,Takeshi Noda,Yoshinori Ohsumi,Yoshinori Ohsumi +14 more
TL;DR: It is shown here that the nature of the association of Apg8 with membranes changes depending on a series of modifications of the protein itself, which appears to be coupled to the membrane dynamics of autophagy and the Cvt pathway.