Related Experiment Video

Updated: May 21, 2025

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

6.8K

Lysine crotonylation in disease: mechanisms, biological functions and therapeutic targets

Yu Ji1, Shanshan Liu1, Yiqiao Zhang1

  • 1Department of General Surgery, Beijing Friendship Hospital, Capital Medical University & State Key Lab of Digestive Health & National Clinical Research Center for Digestive Diseases, Beijing, 100050, China.

Epigenetics & Chromatin
|March 22, 2025
PubMed

Insights

Lysine crotonylation (Kcr), a post-translational modification, regulates key cellular functions and is linked to diseases like cancer. Further research into Kcr mechanisms could offer new therapeutic strategies.

Area of Science:

  • Biochemistry and Molecular Biology
  • Epigenetics
  • Cellular Biology

Background:

  • Lysine crotonylation (Kcr) is an emerging post-translational modification (PTM) involved in fundamental cellular processes.
  • Kcr plays significant roles in gene expression, chromatin remodeling, and cellular metabolism.
  • Dysregulation of Kcr is implicated in various diseases, including cancer and metabolic syndromes.

Purpose of the Study:

  • To review current research on lysine crotonylation (Kcr).
  • To elucidate the regulatory mechanisms and disease associations of Kcr.
  • To highlight future directions for Kcr research in epigenetics and therapeutics.

Main Methods:

  • Literature review and synthesis of existing research on Kcr.
  • Analysis of identified crotonylation sites and regulatory enzymes.
  • Exploration of the interplay between Kcr and other acylation modifications.

Main Results:

  • Kcr is a critical regulator of gene expression, chromatin, and metabolism.
  • Kcr is associated with diverse pathologies, including neurodegenerative disorders, cancer, cardiovascular diseases, and metabolic syndromes.
  • The precise molecular mechanisms of Kcr in disease progression require further investigation.

Conclusions:

  • Understanding Kcr's regulatory roles and disease links is crucial.
  • Investigating the interplay between Kcr and other acylation modifications may yield therapeutic targets.
  • Future research should focus on Kcr's epigenetic roles and therapeutic potential.

More Related Videos

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry12:49

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

11.5K
Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

8.2K

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....
6.7K
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
3.7K
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...
49.6K
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...
12.9K
Feedback Inhibition00:46

Feedback Inhibition

Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!
53.5K
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
2.3K