Protein carboxyl methylation and the biochemistry of memory
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Zhu Li
Abstract
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.
©2009 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Editorial
- Highlight: Molecular and Cellular Mechanisms of Memory
- Highlight: 60th Mosbach Colloquium of the GBM ‘Molecular and Cellular Mechanisms of Memory’
- Protein carboxyl methylation and the biochemistry of memory
- Chemotaxis: how bacteria use memory
- Mechanistic insights in light-induced cAMP production by photoactivated adenylyl cyclase alpha (PACα)
- Balance of power – dynamic regulation of chromatin in plant development
- Ultrafast memory loss and relaxation processes in hydrogen-bonded systems
- Memory and neural networks on the basis of color centers in solids
- Dissection of gene regulatory networks in embryonic stem cells by means of high-throughput sequencing
- The epigenetic bottleneck of neurodegenerative and psychiatric diseases
- Protein Structure and Function
- Mechanism of activation of Saccharomyces cerevisiae calcineurin by Mn2+
- Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation
- Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg257/Lys260, and unmasking of acid-base catalysis
- Genes and Nucleic Acids
- CA/C1 peptidases of the malaria parasites Plasmodium falciparum and P. berghei and their mammalian hosts – a bioinformatical analysis
- Proteolysis
- Placental expression of proteases and their inhibitors in patients with HELLP syndrome
- Irreversible inhibition of human cathepsins B, L, S and K by hypervalent tellurium compounds
Articles in the same Issue
- Editorial
- Highlight: Molecular and Cellular Mechanisms of Memory
- Highlight: 60th Mosbach Colloquium of the GBM ‘Molecular and Cellular Mechanisms of Memory’
- Protein carboxyl methylation and the biochemistry of memory
- Chemotaxis: how bacteria use memory
- Mechanistic insights in light-induced cAMP production by photoactivated adenylyl cyclase alpha (PACα)
- Balance of power – dynamic regulation of chromatin in plant development
- Ultrafast memory loss and relaxation processes in hydrogen-bonded systems
- Memory and neural networks on the basis of color centers in solids
- Dissection of gene regulatory networks in embryonic stem cells by means of high-throughput sequencing
- The epigenetic bottleneck of neurodegenerative and psychiatric diseases
- Protein Structure and Function
- Mechanism of activation of Saccharomyces cerevisiae calcineurin by Mn2+
- Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation
- Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg257/Lys260, and unmasking of acid-base catalysis
- Genes and Nucleic Acids
- CA/C1 peptidases of the malaria parasites Plasmodium falciparum and P. berghei and their mammalian hosts – a bioinformatical analysis
- Proteolysis
- Placental expression of proteases and their inhibitors in patients with HELLP syndrome
- Irreversible inhibition of human cathepsins B, L, S and K by hypervalent tellurium compounds
