Study Data from Osaka University Provide New Insights into Biophysical Research (Optically detected structural change in the N-terminal region of the voltage-sensor domain)
By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Life Science Research. According to news reporting out of Osaka, Japan, by NewsRx editors, research stated, "The voltage-sensor domain (VSD) is a functional module that undergoes structural transitions in response to membrane potential changes and regulates its effectors, thereby playing a crucial role in amplifying and decoding membrane electrical signals. Ion-conductive pore and phosphoinositide phosphatase are the downstream effectors of voltage-gated channels and the voltage-sensing phosphatase, respectively."
Our news journalists obtained a quote from the research from Osaka University, "It is known that upon transition, the VSD generally acts on the region C-terminal to S4. However, whether the VSD also induces any structural changes in the N-terminal region of S1 has not been addressed directly. Here, we report the existence of such an N-terminal effect. We used two distinct optical reporters-one based on the Forster resonance energy transfer between a pair of fluorescent proteins, and the other based on fluorophore-labeled HaloTag-and studied the behavior of these reporters placed at the N-terminal end of the monomeric VSD derived from voltage-sensing phosphatase. We found that both of these reporters were affected by the VSD transition, generating voltage-dependent fluorescence readouts."
According to the news editors, the research concluded: "We also observed that whereas the voltage dependencies of the N-and C-terminal effects appear to be tightly coupled, the local structural rearrangements reflect the way in which the VSD is loaded, demonstrating the flexible nature of the VSD."
For more information on this research see: Optically detected structural change in the N-terminal region of the voltage-sensor domain. Biophysical Journal, 2013;105(1):108-15. (Elsevier - www.elsevier.com; Biophysical Journal - www.elsevier.com/wps/product/cws_home/716950)
Our news journalists report that additional information may be obtained by contacting H. Tsutsui, Laboratory of Integrative Physiology, Graduate School of Medicine, Osaka University, Osaka, Japan. Additional authors for this research include Y. Jinno, A. Tomita and Y. Okamura (see also Life Science Research).
Keywords for this news article include: Asia, Osaka, Japan, Life Science Research.
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