Lipid-anchored protein

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In lipid-anchored proteins, a protein is covalently[1] bonded to a fatty acid such as palmitate or myristate and serves to anchor them to either face of the cell membrane. Examples include bacterial lipoproteins, G proteins and certain kinases. It is believed that the fatty acid chain inserts and assumes a place in the bilayer structure of the membrane alongside the similar fatty-acid tails of the surrounding lipid molecules. Potential points of attachment include the terminal amino group of the protein backbone and the side chain of cysteine residues.

Prenylation is the attachment of lipid chains to proteins to facilitate their interaction with the cell membrane. Some important prenylation chains are geranylgeraniol, farnesol and dolichol, all products of the HMG-CoA reductase metabolic pathway.

Lipid anchored proteins are found within the lipid bilayer. The exact function of the anchor protein has been the subject of much speculation, but it appears to act as an intracellular signal that targets proteins to the apical surface in polarized cells.

Other anchors include the GPI anchor.

References[edit]

  1. ^ Gerald Karp (2009). Cell and Molecular Biology: Concepts and Experiments. John Wiley and Sons. pp. 128–. ISBN 978-0-470-48337-4. Retrieved 13 November 2010.