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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year



Protein carboxyl methylation and the biochemistry of memory

Zhu Li1 / Jeffry B. Stock1, 2

1Signum Biosciences, Inc., Monmouth Junction, NJ 08852, USA

2Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA

Corresponding author

Citation Information: Biological Chemistry. Volume 390, Issue 11, Pages 1087–1096, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2009.133, September 2009

Publication History

Published Online:


Bacterial chemotaxis is mediated by two reversible protein modification chemistries: phosphorylation and carboxyl methylation. Attractants bind to membrane chemoreceptors that control the activity of a protein kinase which acts in turn to control flagellar motor activity. Coordinate changes in receptor carboxyl methylation provide a negative feedback mechanism that serves a memory function. Protein carboxyl methylation might play an analogous role in the nervous system. Two protein carboxyl methyltransferases serve to regulate signal transduction pathways in eukaryotic cells. One is highly expressed in the Purkinje layer of the cerebellum where it methyl esterifies prenylated cysteine residues at the carboxyl-termini of Ras-related and heterotrimeric G-proteins. The other is abundant throughout the brain where it methylates the carboxyl-terminus of protein phosphatase 2A. The phosphatase methyltransferase and the protein methylesterase that reverses phosphatase methylation are structurally related to the corresponding bacterial chemotaxis methylating and demethylating enzymes. Recent results indicate that deficiencies in phosphatase methylation play an important role in the etiology of Alzheimer's disease.

Keywords: Alzheimer's disease; chemotaxis; G-protein; isoprenylcysteine methyltransferase (ICMT); protein phosphatase 2A (PP2A); S-adenosylmethionine

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