Targeting Protein Lipidation in Disease

By M. Resh. 2012

139 citations recorded by the source corpus.

Fatty acids and/or isoprenoids are covalently attached to a variety of disease-related proteins. The distinct chemical properties of each of these hydrophobic moieties allow lipid modification to serve as a mechanism to regulate protein structure, localization and function. This review highlights recent progress in identifying inhibitors of protein lipidation and their effects on human disease. Myristoylation inhibitors have shown promise in blocking the action of human pathogens. Although inhibitors that block prenylation of Ras proteins have not yet been successful for cancer treatment, they may be efficacious in the rare premature aging syndrome progeria. Agents that alter the palmitoylation status of Ras, Wnt and Hh proteins have recently been discovered, and represent the next generation of potential chemotherapeutics.

Subfields: Molecular Biology

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In Molecular Biology

1. Jessica Rios-Esteves
2. M. Resh

Citations in the corpus

• Stearoyl CoA desaturase is required to produce active, lipid-modified Wnt proteins (2013, background): “It is not known why Wnt proteins are modified with palmitoleate instead of palmitate, which is more abundant and is the fatty acid typically attached to “palmitoylated” proteins (Resh, 2012).”