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Related Concept Videos

Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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 affinity and are together...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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.
Sensory organs,...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

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 cells.
Two...
GTPases and their Regulation02:14

GTPases and their Regulation

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.
Large G-proteins, also known...
GTPases and their Regulation02:14

GTPases and their Regulation

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.
Large G-proteins, also known...
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...

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Mapping the Cellular Distribution of an Optogenetic Protein Using a Light-Stimulation Grid
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Guanylyl cyclase sees the light.

John J G Tesmer1

  • 1Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109-2216, USA. johntesmer@umich.edu

Journal of Biology
|November 6, 2008
PubMed
Summary

New atomic structures reveal how enzymes synthesize cyclic guanosine monophosphate (cGMP), a key signaling molecule. This provides insights into substrate specificity and allosteric regulation in nucleotide cyclases.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Cyclic guanosine monophosphate (cGMP) acts as a crucial second messenger in human physiological processes.
  • cGMP plays vital roles in regulating cardiovascular function and vision.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying cGMP synthesis.
  • To investigate the structural basis of substrate specificity and allosteric regulation in nucleotide cyclases.

Main Methods:

  • Determination of atomic structures of cGMP-synthesizing enzymes.
  • Analysis of enzyme structures to understand substrate binding and allosteric effects.

Main Results:

  • Revealed atomic-level details of enzymes responsible for cGMP production.

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Mapping the Cellular Distribution of an Optogenetic Protein Using a Light-Stimulation Grid
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  • Provided new understanding of how these enzymes interact with substrates.
  • Offered insights into the allosteric regulation of nucleotide cyclase activity.

    • Conclusions:

    • The determined enzyme structures offer a molecular foundation for understanding cGMP regulation.
    • These findings pave the way for future research into nucleotide cyclases and their roles in human health.