Hsp20
| Hsp20/alpha crystallin family | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | HSP20 | ||||||||||
| Pfam | PF00011 | ||||||||||
| InterPro | IPR002068 | ||||||||||
| PROSITE | PDOC00791 | ||||||||||
| SCOP2 | 1shs / SCOPe / SUPFAM | ||||||||||
| CDD | cd06464 | ||||||||||
| |||||||||||
Heat shock protein Hsp20 is a family of heat shock proteins. Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp).[1] Amongst them is a family of proteins with an average molecular weight of 20 kDa, known as the hsp20 proteins.[2] These seem to act as 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 know 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]
Human proteins containing this domain
CRYAA; CRYAB; HSPB1; HSPB2; HSPB3; HSPB6; HSPB7; HSPB8; HSPB9;
References
- ^ Lindquist S, Craig EA (1988). "The heat-shock proteins". Annu. Rev. Genet. 22: 631–677. doi:10.1146/annurev.ge.22.120188.003215. PMID 2853609.
- ^ Merck KB, de Jong WW, Bloemendal H, Groenen PJ (1994). "Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology". Eur. J. Biochem. 225 (1): 1–9. doi:10.1111/j.1432-1033.1994.00001.x. PMID 7925426.
- ^ Maaroufi H, Tanguay RM (2013). "Analysis and phylogeny of small heat shock proteins from marine viruses and their cyanobacteria host". PLoS ONE. 8 (11): e81207. doi:10.1371/journal.pone.0081207. PMC 3827213. PMID 24265841.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ LI, D.C.; Lan, Fan; Chen, Dian-Fu; Yang, Wei-Jun; Lu, Bo. "Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2". NCBI. NCBI. Retrieved October 23, 2016.
- ^ G.C, Fan; G, Chu; EG, Kranies. "Hsp20 and its cardioprotection". Pubmed.gov. NCBI. Retrieved October 23, 2016.
- ^ Yan Sin, Yuan; Currie, Susan; P Martin, Lauren; Wills, Tamara; S Baillie, George. "Small heat shock protein 20 (Hsp20) facilitates nuclear import of protein kinase D 1 (PKD1) during cardiac hypertrophy". NCBI. NCBI. Retrieved October 23, 2016.
- ^ M. Dreiza, Catherine; M. Brophy, Colleen; Komalavilas, Padmini; J. Furnish, Elizabeth; Joshi, Lokesh; A. Pallero, Manuel; E. Murphy-Ullrich, Joanne; von Rechenberg, Moritz; J. Ho, Yew-Seng; Richardson, Bonnie; Xu, Nafei; Zhen, Yuejun; M. Peltier, John; Panitch, Alyssa. "Transducible heat shock protein 20 (HSP20) phosphopeptide alters cytoskeletal dynamics". fasebj.org. The FASEB Journal. Retrieved November 6, 2016.
- ^ van Montfort, RL; Basha, E; Friedrich, KL; Slingsby, C; Vierling, E. "Crystal structure and assembly of a eukaryotic small heat shock protein". http://europepmc.org. Europe PMC. Retrieved November 6, 2016.
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