
Aggregation
Autophagy
Ca(2+)
Cancer
Cellular stress
c-Fos
Chaperones
c-myc
Degradation
E3 ligases
Heat shock
Hsp40
Hsp70
Hsp90
Hypoxia
IFN
IGF
Inflammation
LC3
mTor
Neurodegeneration
NFkappaB
Oxidative stress
Parkinson's
Proteases
Proteasome
Protein folding
Protein misfolding
ROS
Tau
Ubiquitin
UPR

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Protein homeostasis and aging: The importance of exquisite quality control
Ageing Res. Rev. 2010, view full abstract in PubMed
All cells count on precise mechanisms that regulate protein homeostasis to maintain a stable and functional proteome. A progressive deterioration in the ability of cells to preserve the stability of their proteome occurs with age and contributes to the functional loss characteristic of old organisms. Molecular chaperones and the proteolytic systems are responsible for this cellular quality control by assuring continuous renewal of intracellular proteins. When protein damage occurs, such as during cellular stress, the coordinated action of these cellular surveillance systems allows detection and repair of the damaged structures or, in many instances, leads to the complete elimination of the altered proteins from inside cells. Dysfunction of the quality control mechanisms and intracellular accumulation of abnormal proteins in the form of protein inclusions and aggregates occur in almost all tissues of an aged organism. Preservation or enhancement of the activity of these surveillance systems until late in life improves their resistance to stress and is sufficient to slow down aging. In this work, we review recent advances on our understanding of the contribution of chaperones and proteolytic systems to the maintenance of cellular homeostasis, the cellular response to stress and ultimately to longevity.