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Related Concept Videos

Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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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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Channel Rhodopsins01:11

Channel Rhodopsins

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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.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
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G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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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.
Sensory...
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Photoreceptors and Visual Pathways01:22

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At the molecular level, visual signals trigger transformations in photopigment molecules, resulting in changes in the photoreceptor cell's membrane potential. The photon's energy level is denoted by its wavelength, with each specific wavelength of visible light associated with a distinct color. The spectral range of visible light, classified as electromagnetic radiation, spans from 380 to 720 nm. Electromagnetic radiation wavelengths exceeding 720 nm fall under the infrared category,...
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IP3/DAG Signaling Pathway01:11

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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The Retina01:32

The Retina

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The retina is a layer of nervous tissue at the back of the eye that transduces light into neural signals. This process, called phototransduction, is carried out by rod and cone photoreceptor cells in the back of the retina.
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Related Experiment Video

Updated: Mar 31, 2026

Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis
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Phosphodiesterase 6D, cGMP-specific rod delta.

Hannah J Gitschier1, Rick H Cote1

  • 1Molecular, Cellular & Biomedical Sciences, University of New Hampshire, NH 03824, US.

The Afcs-Nature Molecule Pages
|October 28, 2015
PubMed
Summary

This study maps protein interactions and functions, revealing key network states and transitions. Understanding these protein pathways and structures aids in predicting cellular functions and evolutionary relationships.

Area of Science:

  • Bioinformatics and Systems Biology
  • Computational Biology and Protein Science

Background:

  • Protein interaction networks are crucial for understanding cellular mechanisms.
  • Identifying conserved protein domains and motifs provides insights into protein function and evolution.

Purpose of the Study:

  • To construct a comprehensive network map of protein states and transitions.
  • To analyze protein classes, sequences, interactions, and pathways.
  • To investigate protein structures, domains, motifs, and orthologs using BLAST data.

Main Methods:

  • Development of a network visualization tool to represent protein states and transitions.
  • Analysis of protein sequence data to identify conserved domains and motifs.
  • Utilizing BLAST for ortholog identification and comparative analysis.

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  • Integration of data on protein interactions, pathways, and structures.

    • Main Results:

    • Detailed mapping of network states and their transitions.
    • Identification of key protein classes and their functional roles within pathways.
    • Characterization of conserved domains and motifs across orthologous proteins.
    • Correlation between protein structure and interaction patterns.

    Conclusions:

    • The constructed network map provides a valuable resource for studying protein interactions and cellular functions.
    • Understanding protein network dynamics is essential for deciphering complex biological processes.
    • This approach facilitates the identification of potential drug targets and biomarkers.