Equilibrated protein homeostasis (referred to as proteostasis)
requires the dynamic coordination of efficient
folding of newly synthesized proteins, quality control and
degradative mechanisms to reduce the load of unfolded
and/or misfolded proteins and thereby prevent abnormal
protein aggregation1
. Protein-folding networks consisting
of cytoplasmic and endoplasmic reticulum (ER)-resident
chaperones ensure proper folding of biologically active
native proteins in a crowded cellular environment that
can reach up to 300–400 grams per litre of proteins2
.
Quality control mechanisms recognize misfolded proteins
and mediate their degradation by the proteasome,
lysosome and macroautophagy pathways