Target type: biologicalprocess
The covalent attachment of a palmitoleyl group to a protein. [GOC:ai]
Protein palmitoleylation is a post-translational modification (PTM) where palmitoleic acid, a monounsaturated fatty acid with a 16-carbon chain and a single cis double bond at the Δ9 position, is attached to a protein. This modification is analogous to palmitoylation, which involves the attachment of palmitic acid, a saturated fatty acid, to proteins.
Palmitoleylation typically occurs on cysteine residues within the protein. The process is catalyzed by palmitoleoyltransferases (PATs), which are a family of enzymes responsible for transferring palmitoleic acid from a donor molecule, such as palmitoleoyl-CoA, to the target protein.
Palmitoleylation serves several important biological functions, including:
- **Membrane Targeting and Anchoring:** Palmitoleylation can promote the association of proteins with cellular membranes, particularly the plasma membrane. This allows for the localization of proteins to specific cellular compartments and facilitates their interaction with other membrane-associated proteins.
- **Protein-Protein Interactions:** Palmitoleylation can influence the interactions between proteins, potentially modulating their activity or stability. The addition of palmitoleoyl groups can create hydrophobic patches on the protein surface, promoting interactions with other hydrophobic regions on other proteins.
- **Signal Transduction:** Palmitoleylation has been implicated in various signal transduction pathways, influencing cellular responses to stimuli. For example, palmitoleylation of certain receptor proteins can modulate their signaling activity, affecting downstream cellular events.
- **Protein Stability and Folding:** Palmitoleylation can contribute to protein stability and proper folding. The attachment of palmitoleic acid can alter the conformation of the protein, promoting its correct folding and reducing its susceptibility to degradation.
- **Cellular Function and Homeostasis:** Palmitoleylation plays a role in diverse cellular processes, including cell growth, differentiation, and metabolism. Alterations in palmitoleylation levels have been linked to various diseases, highlighting its importance in maintaining cellular function and homeostasis.
The biological significance of palmitoleylation is an active area of research. Ongoing studies are exploring the specific roles of this PTM in various cellular processes and its potential implications in health and disease.'
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Protein | Definition | Taxonomy |
---|---|---|
Protein-serine O-palmitoleoyltransferase porcupine | A protein-serine O-palmitoleoyltransferase porcupine that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9H237] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
N-(6-methyl-1,3-benzothiazol-2-yl)-2-[(4-oxo-3-phenyl-6,7-dihydrothieno[3,2-d]pyrimidin-2-yl)thio]acetamide | organic heterobicyclic compound; organonitrogen heterocyclic compound; organosulfur heterocyclic compound | ||
lgk974 | LGK974 : A carboxamide, the structure of which is that of acetamide substituted on carbon by a 2',3-dimethyl-2,4'-bipyridin-5-yl group and on nitrogen by a 5-(pyrazin-2-yl)pyridin-2-yl group. It is a highly potent, selective and orally bioavailable Porcupine inhibitor (a Wnt signalling inhibitor). LGK974: a potent and specific small-molecule inhibitor of Porcupine (PORCN) acyltransferase | bipyridines; pyrazines; pyridines; secondary carboxamide | Wnt signalling inhibitor |
wnt-c59 | 2-(4-(2-methylpyridin-4-yl)phenyl)-N-(4-(pyridin-3-yl)phenyl)acetamide: a PORCN acyltransferase inhibitor; structure in first source |