| basic FUNCTION
| having protein serine/threonine kinase, heat shock protein, transferase activities |
|
displays chaperone activity, autokinase activity, and trigger or block apoptosis activity  |
|
interacts with biological membranes and many different proteins, among them glycolytic enzymes and different protein kinases |
|
possesses chaperonelike activity and prevents aggregation of denatured proteins |
|
HSPB8 activity is intrinsically dependent on BAG3, a protein that may facilitate the disposal of doomed proteins by stimulating macroautophagy |
|
responsible for recognizing the misfolded proteins whereas BAG3, at least in part through its proline-rich domain, might recruit and activate the macroautophagy machinery in close proximity to the chaperone-loaded substrates (MID: 18094623) |
|
bind to unfolded or misfolded proteins and protect them from aggregation |
|
potential role of HSPB8 in ribonucleoprotein processing |
|
promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis |
|
its activity might be implicated in the degradation of several types of neurotoxic proteins accumulating in TARDBP-positive aggregates in most of the cases of sporadic ALS, in some familial ALS not linked to SOD1 mutations, as well as in frontotemporal dementia |
|
having a role in the autophagic removal of misfolded proteins responsible for neurodegenerative diseases |
|
for full HSPB8 activity, autophagy was required although, unlike HSPB7, HSPB8 did induce autophagy |
|
small heat-shock protein implicated in autophagy |
