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Trafficking and signaling by fatty-acylated and prenylated proteins

Nature Chemical Biology volume 2, pages 584–590 (2006)Cite this article

Abstract

A wide variety of signaling proteins are modified by covalently linked fatty acids and/or prenyl groups. These hydrophobic moieties, which include myristate, palmitate, farnesyl and geranylgeranyl, are more than just fat: they provide distinct information that modulates the specificity and efficiency of signal transduction. Recent studies show that lipid modification influences the movement of a signaling protein within the cell and its final destination. Protein lipidation can also confer reversible association with membranes and other signaling proteins. These findings provide new insights into the biochemical and biophysical mechanisms that regulate membrane targeting, trafficking and signaling by lipid-modified proteins.

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Figure 1: Reversible membrane binding of lipid-modified proteins.
Figure 2: Reversible palmitoylation of H-Ras dictates localization and signaling.
Figure 3: Membrane targeting mechanisms for acylated proteins.

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Acknowledgements

Research in the author's laboratory was supported by grants GM57966 and CA72309 from the US National Institutes of Health.

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  1. Cell Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Ave, Box 143, New York, 10021, New York, USA

    Marilyn D Resh

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Resh, M. Trafficking and signaling by fatty-acylated and prenylated proteins. Nat Chem Biol 2, 584–590 (2006). https://doi.org/10.1038/nchembio834

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