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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...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Isolation and Differentiation of Stromal Vascular Cells to Beige/Brite Cells
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Isolation and Differentiation of Stromal Vascular Cells to Beige/Brite Cells

Published on: March 28, 2013

Modulation of PPAR activity via phosphorylation.

Katherine A Burns1, John P Vanden Heuvel

  • 1Department of Veterinary and Biomedical Sciences and Center for Molecular Toxicology and Carcinogenesis, Penn State University, University Park, PA 16802, USA.

Biochimica Et Biophysica Acta
|June 15, 2007
PubMed
Summary

Peroxisome proliferator-activated receptors (PPARs) are crucial nuclear receptors regulating genes for lipid homeostasis, diabetes, and cancer. Their activity is modulated by phosphorylation from various kinases, impacting crucial cellular processes.

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Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

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Last Updated: Jul 14, 2026

Isolation and Differentiation of Stromal Vascular Cells to Beige/Brite Cells
07:22

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Published on: March 28, 2013

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Peroxisome proliferator-activated receptors (PPARs) are nuclear receptors controlling gene expression.
  • Three subtypes (PPARα, β, γ) exist, each with distinct biological roles.
  • PPARs are involved in lipid homeostasis, diabetes, and cancer.

Purpose of the Study:

  • To review the kinases that phosphorylate PPARs.
  • To identify phosphorylation sites and their effects on PPAR activity.
  • To understand how phosphorylation influences PPAR function in various cellular contexts.

Main Methods:

  • Review of existing literature on PPAR phosphorylation.
  • Analysis of kinase-phosphatase cross-talk with PPARs.
  • Examination of phosphorylation effects on ligand binding, DNA binding, coactivator recruitment, and degradation.

Main Results:

  • PPARs are phosphoproteins whose activity is modulated by kinases like ERK, p38-MAPK, PKA, PKC, AMPK, and GSK3.
  • Phosphorylation can occur in a ligand-dependent or -independent manner.
  • The impact of phosphorylation varies based on cellular context, receptor subtype, and specific residue modified.

Conclusions:

  • Phosphorylation is a critical regulatory mechanism for PPAR activity.
  • Understanding these modifications is key to comprehending PPAR's role in metabolic diseases and cancer.
  • Further research into specific kinase-receptor interactions can reveal therapeutic targets.