The voltage sensor of voltage-gated ion channels is a conserved protein domain that senses millivolt changes in transmembrane potential, to regulate ion permeation through the channel. A recently discovered protein, Ci-VSP, has a voltage sensor that is coupled not to an ion channel but to a phosphatidylinositide phosphosphatase, the activity of which depends on membrane potential.
In a new paper published in The Journal of Physiology, Murata and Okamura, from the Okazaki Institute for Integrative Bioscience, examine a voltage-sensitive phosphatase that converts an electrical to a chemical signal; they directly demonstrate that the enzyme activity of Ci-VSP changes in a voltage-dependent manner through the operation of the voltage sensor.
Prior to this work, it was unclear which phosphoinositides were the major substrates of the phosphatase activity, and whether depolarisation or hyperpolarisation induced the phosphatase activity. By expressing phosphoinositide-specific sensors in Xenopus oocytes and applying both electrophysiology and imaging of phosphoinositides, it was shown that enzyme activity is activated upon depolarisation (not upon hyperpolarisation), and that levels of both PtdIns(4,5)P2 and PtsIns(3,4,5)P3 are regulated by the operation of voltage sensor.
“Our findings identify common principles of the voltage sensor shared between voltage-gated ion channels and the voltage-sensing phosphatase," comment the authors.
"There is no question that the VSP is a much simpler model than ion channels for understanding the mechanisms of voltage sensing, and understanding the VSP will provide insights into the function of ion channels as well. Such knowledge is critical for understanding general mechanisms of voltage sensing and many disorders coupled with altered membrane excitabilities. The VSP’s ability to tune phosphoinositide phosphatase activity by voltage will also serve as an important molecular tool to understand mechanisms of tumor suppressor phosphatase, PTEN, and other phosphatases that underlie carcinogenesis and metabolic disorders."
Article: “Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2”, by Yoshimichi Murata and Yasushi Okamura. 15 September 2007, The Journal of Physiology, 583.3, pp. 875–889.
- PHYSICAL SCIENCES
- EARTH SCIENCES
- LIFE SCIENCES
- SOCIAL SCIENCES
Subscribe to the newsletter
Stay in touch with the scientific world!
Know Science And Want To Write?
- Sexual Fantasies: Threesomes Are Normal, Golden Showers Not So Much
- Ghost Light From Dead Galaxies - A Hubble Halloween
- US Wildlife Bans On GMOs And Neonics Lack Transparency And Scientific Rationale
- Is It Possible To Build A Spacesuit Or Spaceship To Travel Through The Sun With Future Tech? - Just For Fun.
- Does Max Tegmark Kill A Daughter In A Parallel World ?
- The Way Architecture Imitates Life, Biology Meets Geometry
- The Vampire Deer Of Afghanistan
- "It's good we are still taking advantage of the bounty of the seas. ..."
- "Except you are all forgetting one MAJOR flaw (esp. in regards to Medicare for all..In the words..."
- "It's alive and well! The Maine Seaweed festival just celebrated the growth of kelp farming in Maine..."
- "Verduyn is right on the money when he says it's not the emotion of sadness itself that's inherently..."
- "A very astute observation, given that they're both, in essence, electrical phenomena...."
- Two-faced anti-GMO groups: Block crop and food innovations then claim Big Ag prevents GMO innovations
- Why support erodes for GMO labeling (Hint: It’s not because of spending by Big Ag)
- Genetic “hall of mirrors” with large palindromes, yet smaller: What’s mighty about the mouse
- Gut bacteria an easy scapegoat for disease, but connections hard to prove
- Vermont Rube Goldberg-like GMO labeling law exempts GMO filled natural supplements
- Downside to GMOs: Yields have become so good, they exceed processing capacity