title: pH-Dependent Assembly and Segregation of the Coiled-Coil Segments of Yeast Putative Cargo Receptors Emp46p and Emp47p.
abstract: Emp46p and Emp47p are yeast putative cargo receptors that recycle between the endoplasmic reticulum and the Golgi apparatus. These receptors can form complexes in a pH-dependent manner, but their molecular mechanisms remain unclear. Here, we successfully reproduced their interactions in vitro solely with their coiled-coil segments, which form stable heterotetramers in the neutral condition but segregate at lower pH. Mutational data identified a key glutamate residue of Emp46p that serves as the pH-sensing switch of their oligomer formation. Our findings elucidate the mechanisms of the dynamic cargo receptor interactions in the secretory pathway and the design framework of the environment-responsive molecular assembly and disassembly systems.
authors.affiliation: Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, Aichi, Japan.
authors.forename: Kentaro
authors.initials: K
authors.lastname: Ishii
authors.affiliation: Graduate School and Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, Japan.
authors.forename: Hiroki
authors.initials: H
authors.lastname: Enda
authors.affiliation: Department of Biotechnology, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
authors.forename: Masanori
authors.initials: M
authors.lastname: Noda
authors.affiliation: Graduate School and Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, Japan.
authors.forename: Megumi
authors.initials: M
authors.lastname: Kajino
authors.affiliation: Graduate School and Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, Japan.
authors.forename: Akemi
authors.initials: A
authors.lastname: Kim
authors.affiliation: Graduate School and Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, Japan; Faculty of Pharmacy, Meijo University, Nagoya, Aichi, Japan.
authors.forename: Eiji
authors.initials: E
authors.lastname: Kurimoto
authors.affiliation: Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo, Japan.
authors.forename: Ken
authors.initials: K
authors.lastname: Sato
authors.affiliation: Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, Wako, Saitama, Japan.
authors.forename: Akihiko
authors.initials: A
authors.lastname: Nakano
authors.affiliation: Department of Biotechnology, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
authors.forename: Yuji
authors.initials: Y
authors.lastname: Kobayashi
authors.affiliation: Graduate School and Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, Japan.
authors.forename: Hirokazu
authors.initials: H
authors.lastname: Yagi
authors.affiliation: Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, Aichi, Japan; Department of Biotechnology, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
authors.forename: Susumu
authors.initials: S
authors.lastname: Uchiyama
authors.affiliation: Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, Aichi, Japan; Graduate School and Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, Japan; Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki, Aichi, Japan.
authors.forename: Koichi
authors.initials: K
authors.lastname: Kato
mesh_terms: D006863:Hydrogen-Ion Concentration; D010446:Peptide Fragments / Q000737:chemistry; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D021381:Protein Transport; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D033921:Vesicular Transport Proteins / Q000737:chemistry*
chemical_list: C473566:EMP46 protein, S cerevisiae; C096914:EMP47 protein, S cerevisiae; D010446:Peptide Fragments; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins