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Related Concept Videos

GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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,...
GPCR Desensitization01:12

GPCR Desensitization

G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
Regulation of Expression Occurs at Multiple Steps02:24

Regulation of Expression Occurs at Multiple Steps

Gene expression can be regulated at almost every step from gene to protein. Transcription is the step that is most commonly regulated. This involves the binding of proteins to short regulatory sequences on the DNA. This association can either promote or inhibit the transcription of a gene associated with the respective sequence.
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Related Experiment Video

Updated: Jun 1, 2026

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein
09:59

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Published on: March 9, 2015

CFTR regulation by phosphorylation.

Rodrigo Alzamora1, J Darwin King, Kenneth R Hallows

  • 1Renal-Electrolyte Division, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA. rra11@pitt.edu

Methods in Molecular Biology (Clifton, N.J.)
|May 20, 2011
PubMed
Summary

Cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel crucial for electrolyte balance. This study details methods for investigating CFTR phosphorylation, a key regulatory mechanism.

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Last Updated: Jun 1, 2026

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein
09:59

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Published on: March 9, 2015

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
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Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
15:12

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae

Published on: May 10, 2014

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • Cystic fibrosis transmembrane conductance regulator (CFTR) is the gene product mutated in cystic fibrosis, a lethal genetic disease.
  • CFTR functions as an ATP-gated, phosphorylation-regulated chloride channel essential for electrolyte transport.
  • CFTR belongs to the ATP-binding cassette (ABC) transporter superfamily and possesses a unique regulatory (R) domain.

Purpose of the Study:

  • To describe strategies and methods for studying CFTR phosphorylation.
  • To provide insights into the regulation of CFTR activity.
  • To facilitate research into cystic fibrosis pathogenesis.

Main Methods:

  • In vitro phosphorylation assays.
  • Whole-cell electrophysiology.
  • Biochemical techniques to analyze CFTR phosphorylation sites.

Main Results:

  • Detailed methodologies for assessing CFTR phosphorylation are presented.
  • The role of various kinases, including PKA and PKC, in CFTR regulation is highlighted.
  • The study provides a framework for understanding CFTR phosphorylation dynamics.

Conclusions:

  • Investigating CFTR phosphorylation is critical for understanding its function and dysfunction in cystic fibrosis.
  • The described methods enable comprehensive analysis of CFTR regulation.
  • This work supports further research into therapeutic strategies targeting CFTR.