Posttranslational arginylation of brain proteins.
The knowledge of brain protein metabolism is important in understanding nervous system brain function. Protein synthesis rates are high in young brain, decline rapidly at adult stages, and thereafter continue falling slowly with age. The breakdown of protein appears to follow a similar rate (1). Protein synthesis and degradation however, are only the two extremes of a complex phenomena which includes a variety of other protein modifications. Proteolytic cleavage is the most common covalent modification of proteins; probably all proteins that have been isolated were modified by proteolysis, since only few are found with the starting amino acid (methionine) attached. This suggests that most proteins were subject to one or more co- and/or posttranslational modifications (2). One of these posttranslational modifications is the arginylation of proteins, described 30 years ago, which now is being recognized as a widespread modification of proteins. In this review, the current status of posttranslational arginylation of brain proteins is discussed.
Hallak
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ME
Centro de Investigaciones en Química Biológica de Córdoba, CI-QUIBIC, (UNC-CONICET), Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Argentina. mhallak@dqbfcq.uncor.edu
Bongiovanni
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D000375:Aging; D016229:Amyloid beta-Peptides / Q000378:metabolism; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D001921:Brain / Q000378:metabolism*; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D014452:Ubiquitins / Q000378:metabolism
D016229:Amyloid beta-Peptides; D008869:Microtubule-Associated Proteins; D009419:Nerve Tissue Proteins; D014452:Ubiquitins; D001120:Arginine