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Related Concept Videos

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Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
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The group Stramenopiles include some phototrophic microorganisms. Members of this group possess flagella covered in numerous short, hairlike extensions, a feature that inspired the group's name, derived from the Latin words for "straw" and "hair." Some of the main categories of Stramenopiles include diatoms, golden algae, and brown algae.Diatoms are unicellular, photosynthetic eukaryotes, with over 200 known genera. They play a key role in the planktonic communities of both marine and...
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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
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Related Experiment Video

Updated: Mar 20, 2026

Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins
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Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins

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Structurally Distinct Cation Channelrhodopsins from Cryptophyte Algae.

Elena G Govorunova1, Oleg A Sineshchekov1, John L Spudich1

  • 1Center for Membrane Biology and Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, McGovern Medical School, Houston, Texas.

Biophysical Journal
|May 29, 2016
PubMed
Summary
This summary is machine-generated.

Cryptophyte algal rhodopsins function as cation channels, not proton pumps, despite sequence similarities to proton pumps. This discovery reveals multiple evolutionary paths for microbial rhodopsin channel function.

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Area of Science:

  • Microbiology
  • Biophysics
  • Molecular Biology

Background:

  • Microbial rhodopsins exhibit diverse functions on a conserved protein scaffold.
  • Cryptophyte algal rhodopsins share sequence homology with haloarchaeal proton pumps, not typical green algal channelrhodopsins.
  • Key aspartate residues, characteristic of proton pumps, are conserved in cryptophyte rhodopsins.

Discussion:

  • Expressed cryptophyte rhodopsins were functionally characterized in human embryonic kidney (HEK293) cells using whole-cell patch-clamp recording.
  • Despite lacking typical channel-associated residues, these proteins facilitate light-gated cation transport.
  • The study demonstrates that these proteins conduct Na(+) and H(+) ions.

Key Insights:

  • Cryptophyte algal rhodopsins function as cation-conducting channelrhodopsins.
  • These channels mediate light-gated passive transport of sodium (Na+) and protons (H+).
  • Rhodopsin channel function has evolved through multiple independent pathways.

Outlook:

  • Further investigation into the structural basis of cryptophyte channelrhodopsin function.
  • Exploring the physiological roles of these unique rhodopsins in cryptophyte algae.
  • Comparative studies to elucidate the diverse evolutionary strategies of microbial rhodopsins.