| Abstract: |
Proteins can be covalently modified with a variety of different lipids, including fatty acids, cholesterol, isoprenoids, phospholipids, and diacylglyceryl lipids. Proteins that are fatty acylated contain amide-linked myristate or thioester-linked palmitate. Alternative modes of fatty acid attachment include amide-linked palmitate (hedgehog proteins) or oxyester-linked palmitoleate or octanoate. Most prenylated proteins are small G proteins containing thioether-linked farnesyl or geranylgeranyl. More than one lipophilic group can be attached to a protein, for example, myristate + palmitate, farnesyl + palmitate or palmitate + cholesterol. In addition, larger and more complex structures are found in mammalian proteins modified with a phospholipid or with a glycosylphosphatidylinositol-anchor and in tri-fatty acylated bacterial lipoproteins. Each of these lipid modifications has been shown to regulate structure, localisation and/or function of the modified proteins. © 2016 Elsevier B.V. All rights reserved. |
