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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

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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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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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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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Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
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Related Experiment Video

Updated: Feb 25, 2026

Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping
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AID Invited to the G4 Summit.

Joseph N Pucella1, Jayanta Chaudhuri1

  • 1Immunology Program, Gerstner Sloan Kettering Graduate School of Biomedical Sciences, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.

Molecular Cell
|August 5, 2017
PubMed
Summary

Researchers identified specific DNA sequences preferred by Activation Induced cytidine Deaminase (AID). This finding clarifies how AID targets DNA during immunoglobulin gene diversification, crucial for adaptive immunity.

Area of Science:

  • Molecular biology
  • Structural biology
  • Immunology

Background:

  • Activation Induced cytidine Deaminase (AID) is essential for adaptive immunity.
  • AID initiates DNA mutations during immunoglobulin diversification.
  • Understanding AID's targeting is key to its mechanisms in somatic hypermutation (SHM) and class switch recombination (CSR).

Purpose of the Study:

  • To identify the specific nucleic acid sequences that are preferred substrates for AID.
  • To elucidate the mechanisms by which AID targets DNA during CSR and SHM.

Main Methods:

  • Biochemical approaches were employed to analyze AID activity.
  • Structural biology techniques were used to determine AID-DNA interactions.

Main Results:

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  • Specific DNA and RNA sequences preferred by AID were identified.
  • The study provides insights into the structural basis of AID targeting.

Conclusions:

  • The findings illuminate the targeting mechanisms of AID during CSR and SHM.
  • This work advances our understanding of immunoglobulin gene diversification.