protein depalmitoleylation

Definition

Target type: biologicalprocess

The removal of palmitoleyl group, a 16-carbon monounsaturated fatty acid (C16:1), from a lipoprotein. [PMID:25731175]

Protein depalmitoleylation is a crucial biological process that involves the removal of palmitoleic acid (C16:1) from a target protein. Palmitoleic acid is a monounsaturated fatty acid that can be attached to proteins through a process called palmitoleoylation. This modification plays a significant role in regulating protein function, localization, and stability.

Depalmitoleylation is catalyzed by a family of enzymes known as palmitoleoyl protein thioesterases (PPTs). PPTs are highly specific enzymes that recognize and cleave the thioester bond between palmitoleic acid and the protein substrate. This reaction typically occurs in the cytoplasm or at the cell membrane.

The removal of palmitoleoyl groups can have a profound impact on protein function. For example, depalmitoleylation can:

- Alter protein localization: Palmitoleylation often targets proteins to specific cellular compartments, such as the plasma membrane or endoplasmic reticulum. Depalmitoleylation can reverse this process, leading to protein translocation to different cellular locations.

- Modify protein activity: Palmitoleylation can influence protein activity by altering its conformation or interactions with other proteins. Depalmitoleylation can restore or disrupt these interactions, affecting protein function.

- Regulate protein stability: Palmitoleylation can enhance protein stability by shielding it from proteolytic degradation. Depalmitoleylation can expose the protein to degradation pathways, leading to its removal from the cell.

In summary, protein depalmitoleylation is a vital regulatory mechanism that controls protein function, localization, and stability. It is a tightly regulated process that involves specific enzymes and plays a critical role in maintaining cellular homeostasis.'
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Proteins (1)

Compounds (5)