The entire life cycle of a protein-from synthesis and folding to
transport and degradation-is carefully controlled by the proteostasis
network. This network, consisting of many interconnected pathways and
processes, manages protein homeostasis by dynamically responding to the
needs of the cell. Stress and aging can challenge the proteostasis
network, resulting in the aggregation of misfolded proteins-a feature of
numerous neurodegenerative conditions.
Written and edited by experts in the field, this collection from Cold
Spring Harbor Perspectives in Biology provides a comprehensive update
on how the proteostasis network functions in healthy cells and the
diseases that result when protein quality control goes awry. The
contributors examine the relevant biochemical attributes of proteins
(e.g., solubility), the functions of normal protein aggregates (e.g.,
biofilm formation in bacteria), and the various heat shock proteins,
chaperones, translocation machineries, proteasomes, signaling factors,
and transcriptional programs involved in proteostasis. The roles of
specific subcellular structures-the endoplasmic reticulum, mitochondria,
ribosomes, lysosomes, and cytoplasm-in protein quality control are
covered, as is the regulation of proteostasis at the organismal level
(e.g., via neuronal activity).
Discussions of the responses by cells when errors in protein quality
control occur, the medical disorders that can result (e.g., Alzheimer
disease), and pharmacologic approaches to ameliorate protein
conformational disorders are also included. This book is therefore an
essential reference for biochemists, cell biologists, and all biomedical
scientists wishing to understand the pathological consequences of and
potential therapies for proteostasis deficiencies in common human
diseases.
