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Related Concept Videos

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,...
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...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.

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Related Experiment Video

Updated: Jul 5, 2026

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

Arrestins as multi-functional signaling adaptors.

V V Gurevich1, E V Gurevich, W M Cleghorn

  • 1Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA. vsevolod.gurevich@vanderbilt.edu

Handbook of Experimental Pharmacology
|May 21, 2008
PubMed
Summary
This summary is machine-generated.

Arrestins regulate cellular signaling by binding to receptors and interacting with diverse proteins. Understanding arrestin conformations and interactions is key to developing new therapies for cancer and neurodegenerative diseases.

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In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

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Last Updated: Jul 5, 2026

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08:21

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

Published on: June 28, 2019

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

In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Pharmacology

Background:

  • Arrestins are crucial regulators of cellular signaling pathways.
  • They bind to phosphorylated G-protein-coupled receptors, modulating signaling and protein interactions.
  • Arrestins interact with over 20 diverse proteins, including kinases and phosphatases, acting as signaling scaffolds.

Purpose of the Study:

  • To explore the therapeutic potential of targeting arrestin interactions.
  • To understand the role of arrestin conformations in cellular signaling.
  • To identify arrestin elements involved in partner interactions for drug development.

Main Methods:

  • Analysis of arrestin interactions with various cellular proteins.
  • Investigation of distinct arrestin conformations (free, receptor-bound, microtubule-bound).
  • Structural elucidation of arrestin-binding interfaces.

Main Results:

  • Arrestins scaffold signaling pathways, including ERK1/2 and JNK3.
  • Arrestin interactions influence cell proliferation, survival, and apoptosis.
  • Distinct arrestin conformations exhibit different signaling capabilities.

Conclusions:

  • Targeting arrestin-dependent signaling offers therapeutic strategies for neurodegenerative diseases and cancer.
  • Understanding arrestin structure-function relationships is vital for designing novel therapeutics.
  • Development of molecular tools and designer arrestins can modulate signaling for disease treatment.