Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Introduction to Actin01:26

Introduction to Actin

Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across different species.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Visual arrestin-1: how did we learn what we know today about this protein?

Progress in retinal and eye research·2026
Same author

Arrestin-3 promotes locomotor sensitization to psychostimulants via JNK signaling in nucleus accumbens.

bioRxiv : the preprint server for biology·2026
Same author

GRKs and arrestins: Nomenclature and functions in GPCR-dependent and -independent signalling.

British journal of pharmacology·2026
Same author

Arrestin-3 sca-olds multiple MAP3Ks driving stress-induced JNK3 activation and cell death.

bioRxiv : the preprint server for biology·2026
Same author

Cytoplasmic tail diversity determines the effector bias of the adhesion GPCR ADGRL2.

Cell chemical biology·2026
Same author

Deceptive beauty of non-natural structures.

Protein science : a publication of the Protein Society·2026
Same journal

Artificial intelligence-driven multi-omics analysis of gut-kidney axis in chronic kidney disease.

Progress in molecular biology and translational science·2026
Same journal

Artificial intelligence in multi-omics analysis of heart diseases.

Progress in molecular biology and translational science·2026
Same journal

AI in multi-omics analysis of type 2 diabetes.

Progress in molecular biology and translational science·2026
Same journal

AI in multi-omics analysis in AMR.

Progress in molecular biology and translational science·2026
Same journal

AI in multi-omics analysis of COVID-19 patient data.

Progress in molecular biology and translational science·2026
Same journal

AI in multi-omics analysis of liver diseases.

Progress in molecular biology and translational science·2026
See all related articles

Related Experiment Video

Updated: May 10, 2026

Parallel Interrogation of β-Arrestin2 Recruitment for Ligand Screening on a GPCR-Wide Scale using PRESTO-Tango Assay
09:03

Parallel Interrogation of β-Arrestin2 Recruitment for Ligand Screening on a GPCR-Wide Scale using PRESTO-Tango Assay

Published on: March 10, 2020

Structural determinants of arrestin functions.

Vsevolod V Gurevich1, Eugenia V Gurevich

  • 1Department of Pharmacology, Vanderbilt University, Nashville, Tennessee, USA.

Progress in Molecular Biology and Translational Science
|June 15, 2013
PubMed
Summary
This summary is machine-generated.

Arrestins are versatile proteins that interact with many cellular components. Understanding their structure allows for engineering arrestins to control specific signaling pathways, offering new therapeutic possibilities.

More Related Videos

Monitoring GPCR-β-arrestin1/2 Interactions in Real Time Living Systems to Accelerate Drug Discovery
08:21

Monitoring GPCR-β-arrestin1/2 Interactions in Real Time Living Systems to Accelerate Drug Discovery

Published on: June 28, 2019

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

Related Experiment Videos

Last Updated: May 10, 2026

Parallel Interrogation of β-Arrestin2 Recruitment for Ligand Screening on a GPCR-Wide Scale using PRESTO-Tango Assay
09:03

Parallel Interrogation of β-Arrestin2 Recruitment for Ligand Screening on a GPCR-Wide Scale using PRESTO-Tango Assay

Published on: March 10, 2020

Monitoring GPCR-β-arrestin1/2 Interactions in Real Time Living Systems to Accelerate Drug Discovery
08:21

Monitoring GPCR-β-arrestin1/2 Interactions in Real Time Living Systems to Accelerate Drug Discovery

Published on: June 28, 2019

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

Area of Science:

  • Molecular biology
  • Cell signaling
  • Protein structure-function relationships

Background:

  • Arrestins are a small protein family crucial for G protein-coupled receptor (GPCR) signaling.
  • They interact with numerous proteins, including GPCRs, signaling molecules, and cytoskeletal elements.
  • The structural basis for arrestin interactions is key to understanding their diverse functions.

Purpose of the Study:

  • To investigate the structural determinants underlying various arrestin functions.
  • To explore the potential for engineering arrestins with specific signaling biases.
  • To provide a foundation for developing novel therapeutic strategies targeting GPCR pathways.

Main Methods:

  • Comprehensive mapping of receptor-binding elements in arrestins.
  • Identification of structural requirements for interactions with non-GPCR binding partners.
  • Construction and analysis of signaling-biased arrestin mutants.

Main Results:

  • Receptor-binding elements in arrestins have been largely mapped, enabling GPCR-specific mutant design.
  • Elements involved in interactions with other proteins are still under investigation.
  • Limited structural insights have already facilitated the development of signaling-biased arrestin mutants.

Conclusions:

  • A deeper understanding of arrestin structure-function relationships is essential.
  • Engineering arrestins can lead to precise control over signaling pathways.
  • This research paves the way for developing novel therapeutics by tailoring arrestin-mediated signaling.