Palmitoylation

The attachment of a 16-carbon saturated fatty acid to Cys residues by a thioether bond is an important mechanism which occurs mostly in the plasma membrane and suggests the regulation of protein function. Identification of sites of palmitoylation on proteins is done through palmitoyl-enriched protein methodology coupled to an FT-ICR MS/MS protocol and/or the use of LC MS/MS via on UPLC LTQ Orbitrap MS instrument.

The enrichment approach (Roth, 2006) can be used to globally monitor palmitoylation changes on large-scale protein preparations, with quantitation using SILAC, DIGE, Label-Free or iTRAQ platforms. The approach can also be utilized as a fractionation technique of complex proteomes and is outlined in the below figure.

Roth, A.F., Wan, J., Bailey, A.O., Sun, B., Kuchar, J.A., Green, W.N., Phinney, B.S., Yates, J.R. 3rd, Davis, N.G. (2006) Global analysis of protein palmitoylation in yeast, Cell. 2006 125:1003-13.

Roth, A.F., Wan, J., Green, W.N., Yates, J.R., Davis, N.G. (2006) Proteomic identification of palmitoylated proteins. Methods. 2006 2:135-42.