Heat Shock Proteins

Symptomatic Relief, Stress Response Pathways, Targeting Heat Shock Proteins

Heat shock proteins are upregulated in response to cellular stresses, including temperature, inflammation, hypoxia, starvation and exposure to toxins. These proteins mainly function as intracellular chaperones, playing an essential role in protein folding and conformation and in preventing protein aggregation. They have also been found to interact with LRRK2 in vivo, and thus may play a role in LRRK2 mutant pathogenicity (Wang et al., 2008).

Reference: 
Wang L, Xie C, Greggio E, Parisiadou L, Shim H, Sun L, et al. The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2. J Neurosci. 2008;28(13):3384-91.
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Contributions:
Related target: TRAP1/hsp75
PARK6 (PINK1)
Holli Kawadler, MJFF
07 May 2009
One identified substrate of PINK1 kinase activity is TRAP1 (heat shock protein 75), an anti-apoptotic mitochondrial chaperone. TRAP1's ability to prevent oxidative stress-induced apoptosis is ... 
Related targets: Chaperones targeting alpha-synuclein toxicity
Targeting Alpha-Synuclein
Holli Kawadler, MJFF
15 Mar 2009
The chaperone Hsp70 was shown to interact with the core hydrophobic region of alpha-synuclein to inhibit fibril assembly (Luk et al, 2008). Geldanamycin (GA) (an Hsp70 inducer) sensitizes the stress ... 
Hsp70 may link parkin activity to alpha-synuclein aggregation
Protein Misfolding & Aggregation
Holli Kawadler, MJFF
10 Mar 2009
Expression of Hsp70 was shown to prevent dopaminergic neuronal loss associated with alpha-synuclein in Drosophila and interference with endogenous chaperone activity accelerated alpha-synuclein toxicity. ... 
Workgroups:
Proteostasis
30 Jun 2009
The proteostasis mechanisms regulate the amount of misfolded proteins (eg, alpha-synuclein) to limit the damage caused by aggregates. In this group, members are encouraged to participate in ...