A
Akihiko Nakano
Researcher at University of Tokyo
Publications - 265
Citations - 17996
Akihiko Nakano is an academic researcher from University of Tokyo. The author has contributed to research in topics: Golgi apparatus & Endoplasmic reticulum. The author has an hindex of 73, co-authored 255 publications receiving 16448 citations. Previous affiliations of Akihiko Nakano include University of California, Berkeley.
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Journal ArticleDOI
The Arabidopsis GNOM ARF-GEF Mediates Endosomal Recycling, Auxin Transport, and Auxin-Dependent Plant Growth
Niko Geldner,Nadine Anders,Hanno Wolters,Jutta Keicher,Wolfgang Kornberger,Philippe Muller,Alain Delbarre,Takashi Ueda,Akihiko Nakano,Gerd Jürgens +9 more
TL;DR: It is demonstrated that GNOM localizes to endosomes and is required for their structural integrity and suggested that ARF-GEFs regulate specific endosomal trafficking pathways.
Journal ArticleDOI
Defensin-like polypeptide LUREs are pollen tube attractants secreted from synergid cells
Satohiro Okuda,Hiroki Tsutsui,Keiko Shiina,Stefanie Sprunck,Hidenori Takeuchi,Ryoko Yui,Ryushiro D. Kasahara,Yuki Hamamura,Akane Mizukami,Daichi Susaki,Nao Kawano,Takashi Sakakibara,Shoko Namiki,Kie Itoh,Kurataka Otsuka,Motomichi Matsuzaki,Hisayoshi Nozaki,Tsuneyoshi Kuroiwa,Akihiko Nakano,Masahiro M. Kanaoka,Thomas Dresselhaus,Narie Sasaki,Tetsuya Higashiyama +22 more
TL;DR: It is reported that secreted, cysteine-rich polypeptides (CRPs) in a subgroup of defensin-like proteins are attractants derived from the synergid cells of T. fournieri, and they showed activity in vitro to attract competent pollen tubes of their own species and were named as LUREs.
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Systematic analysis of SNARE molecules in Arabidopsis: Dissection of the post-Golgi network in plant cells
TL;DR: Possible combinations of SNARE proteins on all subcellular compartments are proposed, and the complexity of the post-Golgi membrane traffic in higher plant cells is suggested.
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Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana.
TL;DR: Examination of green fluorescent protein (GFP)‐tagged proteins indicates that both Ara6 and Ara7 are distributed on a subpopulation of endosomes and suggests their roles in endosomal fusion.
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Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae.
TL;DR: Results suggest that a novel processing mechanism, which might involve a post-translational excision of the internal region followed by peptide ligation, operates on the yeast VMA1 product, and suggest that the vacuolar membrane H(+)-ATPase participates in maintenance of cytoplasmic Ca2+ homeostasis.