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

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.
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.
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

Indirect-Acting Cholinergic Agonists: Mechanism of Action

Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...

You might also read

Related Articles

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

Sort by
Same author

Error analysis of Cm measurement under the whole-cell patch-clamp recording.

Journal of neuroscience methods·2009
Same author

Understanding the self-assembly of charged nanoparticles at the water/oil interface.

Physical chemistry chemical physics : PCCP·2009
Same author

[Development of new SSR markers from EST of SSH cDNA libraries on rose fragrance].

Yi chuan = Hereditas·2009
Same author

Crocin and geniposide profiles and radical scavenging activity of gardenia fruits (Gardenia jasminoides Ellis) from different cultivars and at the various stages of maturation.

Fitoterapia·2009
Same author

Small-molecule screening using a human primary cell model of HIV latency identifies compounds that reverse latency without cellular activation.

The Journal of clinical investigation·2009
Same author

Berberine lowers blood glucose in type 2 diabetes mellitus patients through increasing insulin receptor expression.

Metabolism: clinical and experimental·2009

Related Experiment Video

Updated: Jun 7, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Acetylation modulates prolactin receptor dimerization.

Li Ma1, Jin-song Gao, Yingjie Guan

  • 1Departments of Surgery and Medicine, Brown University School of Medicine-Rhode Island Hospital, Providence, RI 02903, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 22, 2010
PubMed
Summary
This summary is machine-generated.

Prolactin receptor (PRLR) dimerization occurs in the cytoplasm, regulated by acetylation. This process is crucial for activating STAT5 signaling, with acetylation and deacetylation acting as key regulators.

More Related Videos

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Comprehensive Profiling of Dopamine Regulation in Substantia Nigra and Ventral Tegmental Area
09:54

Comprehensive Profiling of Dopamine Regulation in Substantia Nigra and Ventral Tegmental Area

Published on: August 10, 2012

Related Experiment Videos

Last Updated: Jun 7, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Comprehensive Profiling of Dopamine Regulation in Substantia Nigra and Ventral Tegmental Area
09:54

Comprehensive Profiling of Dopamine Regulation in Substantia Nigra and Ventral Tegmental Area

Published on: August 10, 2012

Area of Science:

  • Cellular signaling
  • Molecular biology
  • Biochemistry

Background:

  • Cytokine-activated receptors require extracellular dimerization for intracellular signaling.
  • The prolactin receptor (PRLR) is a key mediator of prolactin signaling.

Purpose of the Study:

  • To investigate the mechanism of prolactin receptor (PRLR) activation.
  • To elucidate the role of acetylation in PRLR cytoplasmic loop dimerization and STAT5 activation.

Main Methods:

  • Cell treatment with prolactin (PRL).
  • Analysis of PRLR and STAT5 acetylation.
  • Inhibition and overexpression of deacetylases (SIRT2, HDAC6).
  • Use of deacetylase inhibitors (nicotinamide, trichostatin A).

Main Results:

  • PRLR undergoes acetylation-dependent cytoplasmic loop dimerization.
  • CREB-binding protein (CBP) acetylates multiple lysine sites on PRLR.
  • Acetylation facilitates PRLR monomer interaction and STAT5 activation.
  • STAT5 also undergoes acetylation-dependent dimerization.
  • Deacetylase inhibition enhances PRLR signaling, while deacetylase expression inhibits it.

Conclusions:

  • Acetylation and deacetylation dynamically regulate PRLR cytoplasmic loop dimerization.
  • This acetylation-dependent mechanism controls STAT5 activation, acting as a rheostat for cytokine receptor signaling.