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Related Concept Videos

Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Generation of Straight or Branched Actin Filaments01:14

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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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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RNA Structure01:19

RNA Structure

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The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
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Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Related Experiment Video

Updated: Sep 22, 2025

Monitoring GPCR-β-arrestin1/2 Interactions in Real Time Living Systems to Accelerate Drug Discovery
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A twist in β-arrestin's tail.

John F Foley1

  • 1Science Signaling, AAAS, Washington, DC 20005, USA.

Science Signaling
|May 24, 2022
PubMed
Summary

Agonist binding and receptor C-tail phosphorylation are essential for G protein-coupled receptors (GPCRs) to recruit and activate β-arrestins, key regulators of receptor signaling.

Area of Science:

  • Cellular signaling
  • Molecular biology
  • Biochemistry

Background:

  • G protein-coupled receptors (GPCRs) are crucial cell surface receptors involved in numerous physiological processes.
  • β-arrestins act as critical adaptors in GPCR signaling, mediating both desensitization and distinct signaling pathways.
  • The precise mechanisms governing GPCR interaction with β-arrestins are complex and involve multiple receptor modifications.

Purpose of the Study:

  • To elucidate the specific requirements for GPCRs to recruit and activate β-arrestins.
  • To investigate the roles of agonist binding and C-tail phosphorylation in β-arrestin interaction.

Main Methods:

  • Biochemical assays to measure protein-protein interactions.
  • Cell-based assays to monitor GPCR signaling and β-arrestin recruitment.

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  • Site-directed mutagenesis to probe the role of C-tail phosphorylation.

    • Main Results:

    • Agonist binding to the GPCR is a prerequisite for β-arrestin recruitment.
    • Phosphorylation of the receptor's C-tail is also necessary for efficient β-arrestin activation.
    • Both events, agonist binding and C-tail phosphorylation, must occur concurrently for robust β-arrestin interaction.

    Conclusions:

    • GPCR activation of β-arrestins is a multi-step process requiring both ligand engagement and post-translational modification.
    • This dual requirement ensures precise spatiotemporal control over β-arrestin-mediated signaling pathways.