Contents. List of Contributors. Preface (A.J. Rivett). Biochemical Properties and Biological Functions of ATP-Dependent Proteases in Bacterial Cells (M.R. Maurizi). From Proteasome to Lysosome: Studies on Yeast Demonstrate the Principles of Protein Degradation in the Eukaryote Cell (M. Thumm and D.H. Wolf). Cellular Regulation by Ubiquitin-Dependent Processes (K.D. Wilkinson). The 20s Proteasome: Subunits and Functions (K. Tanaka and N. Tanahashi). The 19s Regulatory Complex of the 26s Proteasome (W. Dubiel and M. Rechsteiner). Endoplasmic Reticulum0Associated Protein Degradation: an Unconventional Route to a Familiar Fate (A.A. McCracke, E.D. Werner, and J.L. Brodsky). Pathways for the Degradation of Intracellular Proteins within Lysosomes in Higher Eukaryotes (E. Knecht, J.J.M. de Llano, E.J. Andreu, and I.M. Miralles). The Critical Role of the Ubiquitin-proteasome Pathway in Muscle Wasting in Comparison to Lysosomal and Ca2+-dependent Systems (D. Attaix and D. Taillandier). Proteolysis in Apoptosis: Enzymes and Substrates (G.G.F. Mason, and J. Beyette). Index.
This volume brings together a set of reviews that provide a summary of our current knowledge of the proteolytic machinery and of the pathways of protein breakdown of prokaryotic and eukaryotic cells. Intracellular protein degradation is much more than just a mechanism for the removal of incorrectly folded or damaged proteins. Since many short-lived proteins have important regulatory functions, proteolysis makes a significant contribution to many cellular processes including cell cycle regulation and transciptional control. In addition, limited proteolytic cleavage can provide a rapid and efficient mechanism of enzyme activation or inactivation in eukaryotic cells.
In the first chapter, Maurizi provides an introduction to intracellular protein degradation, describes the structure and functions of bacterial ATP-dependent proteases, and explores the relationship between chaperone functions and protein degradation. Many of the principles also apply to eukaryotic cells, although the proteases involved are often not the same. Interestingly, homologues of one of the bacterial proteases, Ion protease, have been found in mitochondria in yeast and mammals, and homologues of proteasomes, which are found in all eukaryotic cells (see below), have been discovered in some eubacteria.
Studies of proteolysis in yeast have contributed greatly to the elucidation of both lysosomal (vacuolar) and nonlysosomal proteolytic pathways in eukaryotic cells. Thumm and Wolf (chapter 2) describe studies that have elucidated the functions of proteasomes in nonlysosomal proteolysis and the contributions of lysosomal proteases to intracellular protein breakdown. Proteins can be selected for degradation by a variety of differen mechanisms. The ubiquitin system is one complex and highly regulated mechanism by which eukaryotic proteins are targetted for degradation by proteosomes. In chapter 3, Wilkinson reviews the components and functions of the ubiquitin system and con
- © Elsevier Science 1998
- 7th August 1998
- Elsevier Science
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Department of Biochemistry, University of Bristol, Bristol, England