Topology-Driven Discovery of Transmembrane Protein -Palmitoylation.

Protein -palmitoylation is a reversible lipophilic posttranslational modification regulating a diverse number of signaling pathways. Within transmembrane proteins (TMPs), -palmitoylation is implicated in conditions from inflammatory disorders to respiratory viral infections. Many small-scale experiments have observed -palmitoylation at juxtamembrane Cys residues.

Analysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap).

Proteins undergo reversible -acylation via a thioester linkage in vivo. -palmitoylation, modification by C16:0 fatty acid, is a common -acylation that mediates critical protein-membrane and protein-protein interactions. The most widely used -acylation assays, including acyl-biotin exchange and acyl resin-assisted capture, utilize blocking of free Cys thiols, hydroxylamine-dependent cleavage of the thioester and subsequent labeling of nascent thiol.

Analysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap).

Proteins undergo reversible -acylation via a thioester linkage in vivo. -palmitoylation, modification by C16:0 fatty acid, is a common -acylation that mediates critical protein-membrane and protein-protein interactions. The most widely used -acylation assays, including acyl-biotin exchange and acyl resin-assisted capture, utilize blocking of free Cys thiols, hydroxylamine-dependent cleavage of the thioester and subsequent labeling of nascent thiol.