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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...
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.
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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.
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GPCRs Regulate Adenylyl Cylase Activity01:09

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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 cells.
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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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G-protein Coupled Receptors01:21

G-protein Coupled Receptors

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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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Published on: October 8, 2015

Probing domain interactions in soluble guanylate cyclase.

Emily R Derbyshire1, Michael B Winter, Mohammed Ibrahim

  • 1Department of Molecular and Cell Biology, University of California-Berkeley, CA 94720, USA.

Biochemistry
|April 16, 2011
PubMed
Summary

Investigating soluble guanylate cyclase (sGC) domains reveals how H-NOX domains influence heme binding and enzyme activity. This research sheds light on the allosteric regulation of H-NOX proteins.

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A Pipeline to Investigate the Structures and Signaling Pathways of Sphingosine 1-Phosphate Receptors

Published on: June 8, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Soluble guanylate cyclase (sGC) is crucial for nitric oxide (NO) signaling by modulating cyclic GMP (cGMP) levels.
  • sGC is a hemoprotein featuring Heme-Nitric oxide and OXygen binding (H-NOX), PAS, coiled-coil, and catalytic domains.
  • Understanding domain roles is key to deciphering sGC's ligand-binding regulation.

Purpose of the Study:

  • To investigate the role of sGC domains in regulating heme cofactor ligand-binding properties.
  • To explore interdomain communication and its effect on heme environment and enzyme activity.
  • To compare the regulatory mechanisms of NO-sensitive sGC and atypical guanylate cyclases.

Main Methods:

  • Construction of chimeric sGC proteins by swapping H-NOX domains with homologous regions from bacterial and worm proteins.
  • Characterization of ligand binding using electronic absorption and resonance Raman spectroscopy.
  • Analysis of cGMP production and enzyme activity in wild-type and mutant sGC constructs.

Main Results:

  • Bacterial and worm H-NOX domains in sGC chimeras were influenced by other sGC domains.
  • Chimeras with bacterial H-NOX domains showed guanylate cyclase activity independent of gaseous ligand binding.
  • Heme pocket mutations and interdomain communication modulated heme-NO complex coordination and oxidation rates.

Conclusions:

  • The study elucidates how different domains within sGC impact heme ligand binding and enzyme regulation.
  • Findings suggest a common molecular mechanism for enzyme activation in atypical and NO-sensitive guanylate cyclases.
  • The research provides insights into the allosteric regulation of H-NOX domain-containing proteins.