Protein prenylation: a new mode of host-pathogen interaction.

Moushimi Amaya, Ancha Baranova, Monique L van Hoek

School of Systems Biology, George Mason University, 10900 University Blvd, Manassas, VA 20110, USA.

Biochemical and biophysical research communications 2011 Dec 9

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Post translational modifications are required for proteins to be fully functional. The three step process, prenylation, leads to farnesylation or geranylgeranylation, which increase the hydrophobicity of the prenylated protein for efficient anchoring into plasma membranes and/or organellar membranes. Prenylated proteins function in a number of signaling and regulatory pathways that are responsible for basic cell operations. Well characterized prenylated proteins include Ras, Rac and Rho. Recently, pathogenic prokaryotic proteins, such as SifA and AnkB, have been shown to be prenylated by eukaryotic host cell machinery, but their functions remain elusive. The identification of other bacterial proteins undergoing this type of host-directed post-translational modification shows promise in elucidating host-pathogen interactions to develop new therapeutics. This review incorporates new advances in the study of protein prenylation into a broader aspect of biology with a focus on host-pathogen interaction. Copyright © 2011 Elsevier Inc. All rights reserved.

Citation

Moushimi Amaya, Ancha Baranova, Monique L van Hoek. Protein prenylation: a new mode of host-pathogen interaction. Biochemical and biophysical research communications. 2011 Dec 9;416(1-2):1-6