peptidyl-lysine glutarylation

Definition

Target type: biologicalprocess

The glutarylation of a lysine residue in a protein. [GOC:sp, PMID:31542297]

Peptidyl-lysine glutarylation is a post-translational modification (PTM) where a glutaryl group (C5H7O3) is attached to the ε-amino group of a lysine residue within a protein. This modification is catalyzed by enzymes called glutaryltransferases, which utilize glutaryl-CoA as a donor molecule.

Glutarylation plays a significant role in various biological processes, including:

* **Regulation of gene expression:** Glutarylation can influence the activity of transcription factors and other proteins involved in gene regulation. For instance, glutarylation of histone proteins can modulate chromatin structure and accessibility, affecting gene expression.
* **Protein stability and degradation:** Glutarylation can affect protein stability and degradation by influencing protein folding, interactions, and recognition by proteasomes.
* **Cellular signaling and communication:** Glutarylation can modify the activity of signaling proteins, influencing cellular responses to stimuli.
* **Metabolic pathways:** Glutarylation can regulate the activity of enzymes involved in metabolic pathways, impacting the flow of metabolites.

The biological significance of glutarylation is further highlighted by its connection to various diseases. Dysregulation of glutarylation has been linked to:

* **Cancer:** Glutarylation has been implicated in cancer development and progression, influencing tumor growth and metastasis.
* **Neurodegenerative diseases:** Dysregulation of glutarylation has been associated with neurodegenerative diseases like Alzheimer's and Parkinson's.
* **Metabolic disorders:** Impaired glutarylation can contribute to metabolic disorders like diabetes and obesity.

Further research is ongoing to elucidate the precise mechanisms and roles of glutarylation in various biological processes and diseases. Understanding these intricacies is crucial for developing targeted therapeutic strategies for treating diseases associated with dysregulation of this modification.'
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Proteins (1)

Compounds (2)