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Books > Science & Mathematics > Biology, life sciences > Cellular biology
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Intracellular Protein Degradation, Volume 27 (Hardcover)
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Intracellular Protein Degradation, Volume 27 (Hardcover)
Series: Advances in Molecular & Cell Biology
Expected to ship within 10 - 15 working days
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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 considers some
of the known substrates for this pathway which include cell cycle
and transcriptional regulators.
The structure and functions of proteosomes and their regulatory
components are described in the two subsequent chapters by Tanaka
and Tanahashi and by Dubiel and Rechsteiner. Proteasomes were the
first known example of threonine proteases. They are multisubunit
complexes that, in addition to being responsible for the turnover
of most short-lived nuclear and cytoplasmic protein, are also
involved in antigen processing for presentation by the MHC class I
pathway. Recent studies reviewed by McCracken and colleagues
(chapter 6) lead to the exciting conclusion that some ER-associated
proteins are degraded by cytosolic proteasomes.
Lysosomes are responsible for the degradation of long-lived
proteins and for the enhanced protein degradation observed under
starvation conditions. In chapter 7 Knecht and colleagues review
the lysosomal proteases and describe studies of the roles of
lysosomes and the mechanisms for protein uptake into lysosomes.
Methods of measuring the relative contribution of different
proteolytic systems (e.g., ubiquitin-proteasome pathway,
calcium-dependent proteases, lysosomes) to muscle protein
degradation, and the conclusions from such studies, are reviewed by
Attai and Taillinder in the following chapter.
Finally, proteases play an important role in signaling apoptosis by
catalyzing the limited cleavage of enzymes. Mason and Beyette
review the role of the major players, caspases, which are both
activated by and catalyze limite proteolysis, and also consider the
involvement of other protoelytic enzymes in this pathway leading
cell death.
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