Special Issue Article
The Protein Lipidation and Its AnalysisGemma Triola*
Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
- *Corresponding Author:
- Dr. Gemma Triola
Department of Chemical Biology
Max Planck Institute of Molecular Physiology
Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
E-mail: [email protected]
Received date: July 05, 2011; Accepted date: September 19, 2011; Published date: September 29, 2011
Citation: Triola G (2011) The Protein Lipidation and Its Analysis. J Glycom Lipidom S2:001. doi: 10.4172/2153-0637.S2-001
Copyright: © 2011 Triola G. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Protein Lipidation is essential not only for membrane binding but also for the interaction with effectors and the regulation of signaling processes, thereby playing a key role in controlling protein localization and function. Cholesterylation, the attachment of the glycosylphosphatidylinositol anchor, as well as N-myristoylation, S-prenylation and S-acylation are among the most relevant protein lipidation processes. Little is still known about the significance of the high diversity in lipid modifications as well as the mechanism by which lipidation controls function and activity of the proteins. Although the development of new strategies to uncover these and other unexplored topics is in great demand, important advances have already been achieved during the last years in the analysis of protein lipidation. This review will highlight the most prominent lipid modifications encountered in proteins and will provide an overview of the existing methods for the analysis and identification of lipid modified proteins.