Shaping proteostasis at the cellular, tissue, and organismal level

AJ Sala, LC Bott, RI Morimoto - Journal of Cell Biology, 2017 - rupress.org
The proteostasis network (PN) regulates protein synthesis, folding, transport, and
degradation to maintain proteome integrity and limit the accumulation of protein aggregates …

The role of co-chaperones in synaptic proteostasis and neurodegenerative disease

EL Gorenberg, SS Chandra - Frontiers in neuroscience, 2017 - frontiersin.org
Synapses must be preserved throughout an organism's lifespan to allow for normal brain
function and behavior. Synapse maintenance is challenging given the long distances …

Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS

P Ciryam, IA Lambert-Smith, DM Bean… - Proceedings of the …, 2017 - National Acad Sciences
Amyotrophic lateral sclerosis (ALS) is a heterogeneous degenerative motor neuron disease
linked to numerous genetic mutations in apparently unrelated proteins. These proteins …

Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program

P Wang, CM Wander, CX Yuan, MS Bereman… - Nature …, 2017 - nature.com
TDP-43 pathology marks a spectrum of multisystem proteinopathies including amyotrophic
lateral sclerosis, frontotemporal lobar degeneration, and sporadic inclusion body myositis …

The heat shock response in neurons and astroglia and its role in neurodegenerative diseases

R San Gil, L Ooi, JJ Yerbury, H Ecroyd - Molecular neurodegeneration, 2017 - Springer
Protein inclusions are a predominant molecular pathology found in numerous
neurodegenerative diseases, including amyotrophic lateral sclerosis and Huntington's …

Molecular chaperone accumulation in cancer and decrease in Alzheimer's disease: the potential roles of HSF1

SK Calderwood, A Murshid - Frontiers in Neuroscience, 2017 - frontiersin.org
Molecular chaperones are required to maintain the proteome in a folded and functional
state. When challenges to intracellular folding occur, the heat shock response is triggered …

Clusterin protects neurons against intracellular proteotoxicity

JM Gregory, DR Whiten, RA Brown, TP Barros… - Acta Neuropathologica …, 2017 - Springer
It is now widely accepted in the field that the normally secreted chaperone clusterin is
redirected to the cytosol during endoplasmic reticulum (ER) stress, although the …

Cellular chaperones as therapeutic targets in ALS to restore protein homeostasis and improve cellular function

B Kalmar, L Greensmith - Frontiers in Molecular Neuroscience, 2017 - frontiersin.org
Heat shock proteins (Hsps) are ubiquitously expressed chaperone proteins that enable cells
to cope with environmental stresses that cause misfolding and denaturation of proteins. With …

Differential HspBP1 expression accounts for the greater vulnerability of neurons than astrocytes to misfolded proteins

T Zhao, Y Hong, P Yin, S Li… - Proceedings of the …, 2017 - National Acad Sciences
Although it is well known that astrocytes are less vulnerable than neurons in
neurodegenerative diseases, the mechanism behind this differential vulnerability is unclear …

A CNS-permeable Hsp90 inhibitor rescues synaptic dysfunction and memory loss in APP-overexpressing Alzheimer's mouse model via an HSF1-mediated …

B Wang, Y Liu, L Huang, J Chen, JJ Li, R Wang… - Molecular …, 2017 - nature.com
Induction of neuroprotective heat-shock proteins via pharmacological Hsp90 inhibitors is
currently being investigated as a potential treatment for neurodegenerative diseases. Two …