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Nanobiology Laboratories Sensory Transduction Group (Prof. Kawamura)
Nanobiology Laboratories Soft Biosystem Group Protonic NanoMachine Group Sensory Transduction Group Biomolecular Networks Laboratories Research Group of Lipid Biosignals Biomolecular Dynamics Group Developmental Biology Group Chromosome Replication Group Integrated Biology Laboratories Laboratory of Genetics Pathology Division KOKORO-Biology Group Cellular Biology Group Organismal Biosystems Laboratories Laboratory of Developmental Immunology Developmental Genetics Group Human Cell Biology Group Medicine and Pathophysiology Group Neuroscience Laboratories Visual Neuroscience Group Developmental and Functional Neuroscience Group Cognitive Neuroscience Group Cellular and Molecular Neurobiology Group Synaptic Plasticity Group Biophysical Dynamics Laboratories Physiological Laboratory Nonequilibrium Physics Group Functional Proteomics Group Nano-Biophotonics Group Biomedical Engineering Laboratories Systems Neuroscience Group Department of Molecular Genetics Laboratory of Intercellular Communications Laboratory of Stem Cell Research Laboratory of Protein Informatics Laboratory of Biocatalysis Science Collaborative institutes Laboratory of Immune Regulation Chugai Pharmaceutical CO.,LTD. Optical Nano Device Group OMRON Corporation Name Email Telephone HP Professor KAWAMURA Satoru +81-6-6879-4610 HP Associate Prof. TACHIBANAKI Shuji +81-6-6879-4613 HP Assistant Prof. WADA Yasutaka +81-6-6879-4611   TEL (Lab.) +81-6-6879-4612 FAX +81-6-6879-4614 Postal Mail Address Sensory Transduction Group, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoaka, Suita, Osaka 565-0871, JAPAN For more information http://www.bio.sci.osaka-u.ac.jp/~kawamura/English%20page.htm Detection of light in photoreceptors is attained through a phototransduction cascade. We are interested in how the sensitivity is determined in the cascade and how the necessary components are localized at the appropriate cellular compartments. 1 Molecular mechanisms that characterize cone photoresponses. Cones are less light-sensitive than rods, and the light response of a cone is much briefer than that of a rod. Using isolated rods and cones, we will study biochemically the mechanisms how these differences come from. 2 Mechanism of S-modulin action. S-modulin is a calcium-binding protein that inhibits rhodopsin kinase (RK) at high calcium concentrations in the dark. Since rhodopsin phosphorylation is a mechanism that quenches the light-activated rhodopsin, its inhibition is thought to increase the sensitivity of a photoreceptor to light. We will study the interaction sites of both S-modulin and RK. 3 Function and functional mechanism of a novel calcium-binding protein, p26. A calcium-binding protein, p26, was initially found in frog olfactory cilia (originally named as p26olf). This protein consists of two S100 domains aligned in tandem. Since S100 proteins are thought to be functional in a dimer form, p26 is probably functional with its own. We will study the function and its mechanism of this protein in calcium signaling in olfactory cells and other cells.

 

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