Hsp20
| Hsp20/alpha crystallin family | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | HSP20 | ||||||||||
SCOP2 | 1shs / SCOPe / SUPFAM | ||||||||||
| CDD | cd06464 | ||||||||||
| |||||||||||
The heat shock protein Hsp20 family, also known as small heat shock proteins (sHSPs), is a
heat shock proteins
.
Prokaryotic and eukaryotic organisms respond to
protein chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Structurally, this family is characterised by the presence of a conserved C-terminal domain, alpha-crystallin domain, of about 100 residues. Recently, small heat shock proteins (sHSPs) were found in marine viruses (cyanophages).[3]
Function and regulation
Hsp20, like all heat shock proteins, is in abundance when cells are under stressed conditions.[4] Hsp20 is known to be expressed in many human tissues, including the brain and heart.[5] Hsp20 has been studied extensively in cardiac myocytes and is known to act as a chaperon protein, binding to protein kinase 1 (PDK1) and allowing its nuclear transport.[6] In addition, the phosphorylation of hsp20 has been shown to effect the structure of cells cytoskeletons.[7] Due to hsp20 commonly forming dimers with itself when heated, its function of chaperoning can be greatly affected.[8]