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115 results on '"Yanagisawa, Haruaki"'

7. TTC26/DYF13 is an intraflagellar transport protein required for transport of motility-related proteins into flagella

Author

Ishikawa, Hiroaki, Ide, Takahiro, Yagi, Toshiki, Jiang, Xue, Hirono, Masafumi, Sasaki, Hiroyuki, Yanagisawa, Haruaki, Wemmer, Kimberly A, Stainier, Didier YR, Qin, Hongmin, Kamiya, Ritsu, and Marshall, Wallace F

Subjects
Biochemistry and Cell Biology, Bioinformatics and Computational Biology, Biological Sciences, 1.1 Normal biological development and functioning, Underpinning research, Generic health relevance, Algal Proteins, Animals, Carrier Proteins, Cell Line, Cell Movement, Chlamydomonas reinhardtii, Cilia, Embryo, Nonmammalian, Flagella, Gene Expression Regulation, Developmental, Gene Knockdown Techniques, Genotype, Intracellular Signaling Peptides and Proteins, Mice, Mutation, Phenotype, Plant Proteins, Protein Transport, Transfection, Zebrafish, Zebrafish Proteins, Chlamydomonas, axoneme, dynein, flagella, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract

Cilia/flagella are assembled and maintained by the process of intraflagellar transport (IFT), a highly conserved mechanism involving more than 20 IFT proteins. However, the functions of individual IFT proteins are mostly unclear. To help address this issue, we focused on a putative IFT protein TTC26/DYF13. Using live imaging and biochemical approaches we show that TTC26/DYF13 is an IFT complex B protein in mammalian cells and Chlamydomonas reinhardtii. Knockdown of TTC26/DYF13 in zebrafish embryos or mutation of TTC26/DYF13 in C. reinhardtii, produced short cilia with abnormal motility. Surprisingly, IFT particle assembly and speed were normal in dyf13 mutant flagella, unlike in other IFT complex B mutants. Proteomic and biochemical analyses indicated a particular set of proteins involved in motility was specifically depleted in the dyf13 mutant. These results support the concept that different IFT proteins are responsible for different cargo subsets, providing a possible explanation for the complexity of the IFT machinery. DOI: http://dx.doi.org/10.7554/eLife.01566.001.

Published
2014

9. Cryo-EM structures of the human volume-regulated anion channel LRRC8

Author

Kasuya, Go, Nakane, Takanori, Yokoyama, Takeshi, Jia, Yanyan, Inoue, Masato, Watanabe, Kengo, Nakamura, Ryoki, Nishizawa, Tomohiro, Kusakizako, Tsukasa, Tsutsumi, Akihisa, Yanagisawa, Haruaki, Dohmae, Naoshi, Hattori, Motoyuki, Ichijo, Hidenori, Yan, Zhiqiang, Kikkawa, Masahide, Shirouzu, Mikako, Ishitani, Ryuichiro, and Nureki, Osamu

Published
2018
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24. Cryo-electron tomography of cardiac myofibrils reveals a contraction-induced lattice twist in the Z-discs

Author

Oda, Toshiyuki and Yanagisawa, Haruaki

Subjects
Striated muscle tissue, Materials science, macromolecular substances, Sarcomere, law.invention, law, medicine, Biophysics, Cryo-electron tomography, Elasticity (economics), medicine.symptom, Electron microscope, Myofibril, Actin, Muscle contraction
Abstract

The Z-disc forms a boundary between sarcomeres, which constitute structural and functional units of striated muscle tissue. Actin filaments from adjacent sarcomeres are cross-bridged by α-actinin in the Z-disc, allowing transmission of tension across the myofibril. Despite decades of studies, the 3D structure of Z-disc has been elusive due to the limited resolution of conventional electron microscopy. Here, we observed porcine cardiac myofibrils using cryo-electron tomography and reconstructed the 3D structures of the actinactinin cross-bridging complexes within the Z-discs in relaxed and activated states. We found that the α-actinin showed a contraction-induced swing motion along with a global twist in the actin lattice. Our observation suggests that the elasticity and the integrity of the Z-disc during the muscle contraction cycle are maintained by the structural flexibility within the actin-actinin complex.

Published
2020
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26. Alternating Heterochiral Supramolecular Copolymerization

Author

Ueda, Michihisa, primary, Aoki, Tsubasa, additional, Akiyama, Takayoshi, additional, Nakamuro, Takayuki, additional, Yamashita, Keitaro, additional, Yanagisawa, Haruaki, additional, Nureki, Osamu, additional, Kikkawa, Masahide, additional, Nakamura, Eiichi, additional, Aida, Takuzo, additional, and Itoh, Yoshimitsu, additional

Published
2021
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34. Cryo-EM structure of the volume-regulated anion channel LRRC8

Author

Kasuya, Go, primary, Nakane, Takanori, additional, Yokoyama, Takeshi, additional, Jia, Yanyan, additional, Inoue, Masato, additional, Watanabe, Kengo, additional, Nakamura, Ryoki, additional, Nishizawa, Tomohiro, additional, Kusakizako, Tsukasa, additional, Tsutsumi, Akihisa, additional, Yanagisawa, Haruaki, additional, Dohmae, Naoshi, additional, Hattori, Motoyuki, additional, Ichijo, Hidenori, additional, Yan, Zhiqiang, additional, Kikkawa, Masahide, additional, Shirouzu, Mikako, additional, Ishitani, Ryuichiro, additional, and Nureki, Osamu, additional

Published
2018
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35. Spiro-Conjugated Carbon/Heteroatom-Bridged p-Phenylenevinylenes: Synthesis, Properties, and Microcrystal Electron Crystallographic Analysis of Racemic Solid Solutions

Author

Hamada, Hiroyoshi, Nakamuro, Takayuki, Yamashita, Keitaro, Yanagisawa, Haruaki, Nureki, Osamu, Kikkawa, Masahide, Harano, Koji, Shang, Rui, and Nakamura, Eiichi

Abstract

Two planar conjugated systems perpendicularly connected via a quaternary sp3carbon center interact with each other through the spiro linkage. Such spiro-conjugated p-systems show useful optoelectronic properties. Herein, we present a unified modular synthetic strategy for a series of chiral spiro-conjugated carbocycles utilizing a C–H activation reaction as a key step. The chiral spiro-conjugated carbon/heteroatom-bridged p-phenylenevinylenes (spiro-Xcompounds) possessing C, O, N, S, and SO2as bridging groups are thermally stable, and exhibit circular dichroism and circularly polarized luminescence (CPL). Spiro-SO2undergoes intramolecular charge transfer. It exhibits CPL with a large |glum| of 2.1 × 10-3and shows rarely reported solvatofluorochromism for CPL luminophores. The racemic spiro-Ocompound solidifies as a racemic solid solution (or pseudoracemate). It did not form X-ray-quality crystals. This therefore provided us with a unique opportunity to examine the potential of the microcrystal electron crystallography popularized recently. The diffraction data sets, merged over many micrometer-sized solid particles, afforded the 3D molecular structure and the crystal packing of the spiro compound.Spiro-conjugated carbon/heteroatom-bridged p-phenylenevinylenes were synthesized via a modular synthetic route, utilizing C–H activation as a key step. They exhibited circularly polarized luminescence, and formed racemic solid solutions (or pseudoracemates) as elucidated by microcrystal electron crystallography.

Published
2020
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37. Bioconjugation of Au25Nanocluster to Monoclonal Antibody at Tryptophan

Author

Malawska, Katarzyna Joanna, Takano, Shinjiro, Oisaki, Kounosuke, Yanagisawa, Haruaki, Kikkawa, Masahide, Tsukuda, Tatsuya, and Kanai, Motomu

Abstract

We report the first bioconjugation of Au25nanocluster to a monoclonal antibody at scarcely exposed tryptophan (Trp) residues toward the development of high-resolution probes for cryogenic electron microscopy (cryo-EM) and tomography (cryo-ET). To achieve this, we improved the Trp-selective bioconjugation using hydroxylamine (ABNOH) reagents instead of previously developed N-oxyl radicals (ABNO). This new protocol allowed for the application of Trp-selective bioconjugation to acid-sensitive proteins such as antibodies. We found that a two-step procedure utilizing first Trp-selective bioconjugation for the introduction of azide groups to the protein and then strain-promoted azide-alkyne cycloaddition (SPAAC) to attach a bicyclononyne (BCN)-presenting redox-sensitive Au25nanocluster was essential for a scalable procedure. Covalent labeling of the antibody with gold nanoclusters was confirmed by various analytical methods, including cryo-EM analysis of the Au25nanocluster conjugates.

Published
2024
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42. Correction: TTC26/DYF13 is an intraflagellar transport protein required for transport of motility-related proteins into flagella

Author

Ishikawa, Hiroaki, primary, Ide, Takahiro, additional, Yagi, Toshiki, additional, Jiang, Xue, additional, Hirono, Masafumi, additional, Sasaki, Hiroyuki, additional, Yanagisawa, Haruaki, additional, Wemmer, Kimberly A, additional, Stainier, Didier YR, additional, Qin, Hongmin, additional, Kamiya, Ritsu, additional, and Marshall, Wallace F, additional

Published
2014
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44. Author response: TTC26/DYF13 is an intraflagellar transport protein required for transport of motility-related proteins into flagella

Author

Ishikawa, Hiroaki, primary, Ide, Takahiro, additional, Yagi, Toshiki, additional, Jiang, Xue, additional, Hirono, Masafumi, additional, Sasaki, Hiroyuki, additional, Yanagisawa, Haruaki, additional, Wemmer, Kimberly A, additional, Stainier, Didier YR, additional, Qin, Hongmin, additional, Kamiya, Ritsu, additional, and Marshall, Wallace F, additional

Published
2014
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49. Unveiling Liquid-Crystalline Lipids in the Urothelial Membrane through Cryo-EM.

Author

Yanagisawa H, Kita Y, Oda T, and Kikkawa M

Abstract

The urothelium, a distinct epithelial tissue lining the urinary tract, serves as an essential component in preserving urinary tract integrity and thwarting infections. The asymmetric unit membrane (AUM), primarily composed of the uroplakin complex, constitutes a critical permeability barrier in fulfilling this role. However, the molecular architectures of both the AUM and the uroplakin complex have remained enigmatic due to the paucity of high-resolution structural data. In this study, we utilized cryo-electron microscopy to elucidate the three-dimensional structure of the uroplakin complex within the porcine AUM. While the global resolution achieved was 3.5 Å, we acknowledge that due to orientation bias, the resolution in the vertical direction was determined to be 6.3 Å. Our findings unveiled that the uroplakin complexes are situated within hexagonally arranged crystalline lipid membrane domains, rich in hexosylceramides. Moreover, our research rectifies a misconception in a previous model by confirming the existence of a domain initially believed to be absent, and pinpointing the accurate location of a crucial Escherichia coli binding site implicated in urinary tract infections. These discoveries offer valuable insights into the molecular underpinnings governing the permeability barrier function of the urothelium and the orchestrated lipid phase formation within the plasma membrane.

Published
2023
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50. Unveiling Liquid-Crystalline Lipids in the Urothelial Membrane through Cryo-EM.

Author

Oda T, Yanagisawa H, Kikkawa M, and Kita Y

Abstract

The urothelium, a distinct epithelial tissue lining the urinary tract, serves as an essential component in preserving urinary tract integrity and thwarting infections. The asymmetric unit membrane (AUM), primarily composed of the uroplakin complex, constitutes a critical permeability barrier in fulfilling this role. However, the molecular architectures of both the AUM and the uroplakin complex have remained enigmatic due to the paucity of high-resolution structural data. In this investigation, we employed cryo-electron microscopy to elucidate the three-dimensional structure of the uroplakin complex embedded within the porcine AUM at a resolution of 3.5 Å. Our findings unveiled that the uroplakin complexes are situated within hexagonally arranged crystalline lipid membrane domains, rich in hexosylceramides. Moreover, our research rectifies a misconception in a previous model by confirming the existence of a domain initially believed to be absent, and pinpointing the accurate location of a crucial Escherichia coli binding site implicated in urinary tract infections. These discoveries offer valuable insights into the molecular underpinnings governing the permeability barrier function of the urothelium and the orchestrated lipid phase formation within the plasma membrane.

Published
2023
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