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Related Concept Videos

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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
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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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G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
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Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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Mapping the Cellular Distribution of an Optogenetic Protein Using a Light-Stimulation Grid
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Mapping the Cellular Distribution of an Optogenetic Protein Using a Light-Stimulation Grid

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An engineered membrane-bound guanylyl cyclase with light-switchable activity.

Yuehui Tian1,2, Georg Nagel3, Shiqiang Gao4

  • 1Department of Neurophysiology, Institute of Physiology, Biocenter, University of Wuerzburg, 97070, Wuerzburg, Germany.

BMC Biology
|March 29, 2021
PubMed
Summary
This summary is machine-generated.

Scientists engineered a novel light-switchable guanylyl cyclase (GC) enzyme. This switch-Cyclop1 enzyme allows for precise, non-invasive control of cyclic GMP (cGMP) levels using light flashes.

Keywords:
Chlamydomonas reinhardtiiCyclic GMPGuanylyl cyclaseOptogeneticsRhodopsin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Optogenetics

Background:

  • Microbial rhodopsins exhibit diverse functions, including light-sensitive ion transport and enzymatic activities.
  • A novel family of two-component Cyclase (rhod)opsins (2c-Cyclop) was identified, displaying light-inhibited guanylyl cyclase (GC) activity.
  • The functions of many 2c-Cyclop homologs in algal genomes remained uncharacterized.

Purpose of the Study:

  • To engineer a light-switchable guanylyl cyclase (GC) for precise control of cyclic GMP (cGMP) levels.
  • To investigate the light-sensitivity and switching properties of the engineered enzyme.
  • To establish a tool for non-invasive investigation of cGMP signaling pathways.

Main Methods:

  • Chlamyopsin-5 (Cop5) and a related guanylyl cyclase Cr2c-Cyclop1 from Chlamydomonas reinhardtii were used.
  • Parts of Cop5 and Cr2c-Cyclop1 were exchanged to create a chimeric protein, switch-Cyclop1.
  • The activity of switch-Cyclop1 was measured in Xenopus laevis oocytes under different light conditions.

Main Results:

  • An engineered bi-stable guanylyl cyclase, switch-Cyclop1, was created by swapping opsin domains.
  • switch-Cyclop1 activity is reversibly switched by light: activated by 380 nm light and inhibited by blue/green light.
  • The enzyme exhibits high light-sensitivity, with activation and inhibition occurring at low photon densities.

Conclusions:

  • The engineered switch-Cyclop1 is the first light-switchable enzyme for regulating cGMP levels.
  • This enzyme provides a novel, highly light-sensitive method for non-invasive control of cGMP production.
  • The tool holds promise for studying the physiological effects of cGMP signaling in various tissues.