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Alberts B, Johnson A, Lewis J, et al. Molecular Biology of the Cell. 4th edition. New York: Garland Science; 2002.

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Molecular Biology of the Cell. 4th edition.

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Figure 10-18. Membrane protein attachment by a fatty acid chain or a prenyl group.

Figure 10-18Membrane protein attachment by a fatty acid chain or a prenyl group

The covalent attachment of either type of lipid can help localize a water-soluble protein to a membrane after its synthesis in the cytosol. (A) A fatty acid chain (myristic acid) is attached via an amide linkage to an N-terminal glycine. (B) A prenyl group (either farnesyl or a longer geranylgeranyl group) is attached via a thioether linkage to a cysteine residue that is initially located four residues from the protein's C-terminus. After this prenylation, the terminal three amino acids are cleaved off, and the new C-terminus is methylated before insertion into the membrane. Palmitic acid, an 18 carbon saturated fatty acid, can also be attached to some proteins via thioester bonds formed with internal cysteine side chains. This modification is often reversible, allowing proteins to become recruited to membranes only when needed. The structures of two lipid anchors are shown below: (C) a myristyl anchor (a 14-carbon saturated fatty acid chain), and (D) a farnesyl anchor (a 15-carbon unsaturated hydrocarbon chain).

From: Membrane Proteins

Copyright © 2002, Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, and Peter Walter; Copyright © 1983, 1989, 1994, Bruce Alberts, Dennis Bray, Julian Lewis, Martin Raff, Keith Roberts, and James D. Watson .

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