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Nanobiology Laboratories Sensory Transduction Group (Prof. Kawamura)

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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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