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

The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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...
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...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...

You might also read

Related Articles

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

Sort by
Same author

[Consensus paper for the standardized laboratory diagnostics of chronic kidney disease (CKD) in the context of cardiovascular-renal-metabolic health (ÖGLMKC, ÖQUASTA, ÖGN) : Consensus paper of the Austrian Society for Laboratory Medicine and Clinical Chemistry (ÖGLMKC), the Austrian Society for Quality Assurance and Standardization of Medical Diagnostic Examinations (ÖQUASTA), and the Austrian Society for Nephrology (ÖGN)].

Wiener klinische Wochenschrift·2026
Same author

The Protein Phosphatase Inhibitor LB100 Targets the Mesenchymal Lineage of Pancreatic Ductal Adenocarcinoma.

MedComm·2026
Same author

Engineering Nanoscale Frontiers: Valve Metal Oxide Nanostructures From Fundamentals to Multifunctional Biomedical Applications.

Chemical record (New York, N.Y.)·2026
Same author

Dual FLT3/MAPK14 Proteolysis-Targeting Chimera (PROTAC) Induces Potent Acute Myeloid Leukemia Cell Death.

Pharmaceuticals (Basel, Switzerland)·2026
Same author

The Host Cell Factor Phosphatase-2A Subunit PR130 Restricts Replication of Herpes Simplex Virus Type-1.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Dual inhibition of PP2A and WEE1 induces apoptosis and mitotic catastrophe in cancer cells.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2026

Related Experiment Video

Updated: Jun 26, 2026

Chromatin Immunoprecipitation (ChIP) to Assay Dynamic Histone Modification in Activated Gene Expression in Human Cells
13:20

Chromatin Immunoprecipitation (ChIP) to Assay Dynamic Histone Modification in Activated Gene Expression in Human Cells

Published on: July 29, 2010

A phosphorylation-acetylation switch regulates STAT1 signaling.

Oliver H Krämer1, Shirley K Knauer, Georg Greiner

  • 1Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine (CMB), University of Jena, 07743 Jena, Germany. Oliver.Kraemer@uni-jena.de

Genes & Development
|January 28, 2009
PubMed
Summary

STAT1 acetylation counteracts interferon signaling by inhibiting phosphorylation, nuclear translocation, and gene expression. This phospho-acetyl switch involves CBP, HDAC3, and TCP45, revealing a new regulatory layer in cytokine signaling.

More Related Videos

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Time-resolved Förster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells
07:12

Time-resolved Förster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells

Published on: September 9, 2021

Related Experiment Videos

Last Updated: Jun 26, 2026

Chromatin Immunoprecipitation (ChIP) to Assay Dynamic Histone Modification in Activated Gene Expression in Human Cells
13:20

Chromatin Immunoprecipitation (ChIP) to Assay Dynamic Histone Modification in Activated Gene Expression in Human Cells

Published on: July 29, 2010

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Time-resolved Förster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells
07:12

Time-resolved Förster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells

Published on: September 9, 2021

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Epigenetics

Background:

  • Cytokines like interferons (IFNs) activate signal transducers and activators of transcription (STATs) through phosphorylation.
  • Histone deacetylases (HDACs) and histone acetyltransferase (HAT) CBP dynamically regulate STAT1 acetylation.
  • STAT1 acetylation's role in modulating IFN signaling remains incompletely understood.

Purpose of the Study:

  • To elucidate the role of STAT1 acetylation in regulating interferon-induced STAT1 signaling.
  • To identify the key molecular players involved in the STAT1 phospho-acetyl switch.
  • To investigate the distinct functions of CBP-mediated acetylation in STAT1 signaling.

Main Methods:

  • Biochemical assays to assess STAT1 phosphorylation and acetylation.
  • Genetic manipulation to alter HAT/HDAC activity ratios.
  • Analysis of STAT1 mutants to understand the phospho-acetyl switch mechanism.
  • Co-immunoprecipitation and phosphatase assays to study protein interactions.

Main Results:

  • STAT1 acetylation antagonizes IFN-induced STAT1 phosphorylation, nuclear translocation, DNA binding, and target gene expression.
  • A phospho-acetyl switch, regulated by CBP, HDAC3, and TCP45, controls STAT1 signaling.
  • CBP-mediated acetylation inhibits STAT1 signaling independently of its transcriptional activation functions.
  • STAT1 acetylation promotes binding of TCP45, which dephosphorylates and inactivates STAT1.

Conclusions:

  • STAT1 acetylation represents a novel regulatory mechanism that counteracts cytokine signaling.
  • The interplay between STAT1 phosphorylation and acetylation, mediated by a specific set of enzymes, fine-tunes STAT1 activity.
  • This discovery adds a new layer to our understanding of STAT1 modulation and cytokine signal transduction.