PF00183

Hsp90 protein

Pfam entry
Member databasePfam
Pfam typefamily
Short nameHSP90
Author Finn RD;0000-0001-8626-2148
Sequence Ontology0100021

Description
Imported from IPR001404

Molecular chaperones, or heat shock proteins (Hsps) are ubiquitous proteins that act to maintain proper protein folding within the cell
[1]
. They assist in the folding of nascent polypeptide chains, and are also involved in the refolding of denatured proteins following proteotoxic stress. As their name implies, the heat shock proteins were first identified as proteins that were up-regulated under conditions of elevated temperature. However, subsequent studies have shown that increased Hsp expression is induced by a variety of cellular stresses, including oxidative stress and inflammation. Five major Hsp families have been determined, and are categorized according to their molecular size (Hsp100, Hsp90, Hsp70, Hsp60, and the small Hsps). Hsps are involved in a variety of cellular processes that are ATP-dependent. These include: prevention of protein aggregation, protein degradation, protein trafficking, and maintenance of signalling proteins in a conformation that permits activation.

Hsp90 chaperones are unique in their ability to regulate a specific subset of cellular signalling proteins that have been implicated in disease processes, including intracellular protein kinases, steroid hormone receptors, and growth factor receptors
[2, 4, 5, 6, 8, 7, 3]
.

References
Imported from IPR001404

1.Microbial molecular chaperones. Lund PA. Adv. Microb. Physiol. 44, 93-140, (2001). View articlePMID: 11407116

2.The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Pratt WB. Proc. Soc. Exp. Biol. Med. 217, 420-34, (1998). View articlePMID: 9521088

3.Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Johnson JL. Biochim Biophys Acta 1823, 607-13, (2012). PMID: 22008467

4.Hsp90 and co-chaperones twist the functions of diverse client proteins. Zuehlke A, Johnson JL. Biopolymers 93, 211-7, (2010). PMID: 19697319

5.Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA, Agard DA. Mol Cell 53, 330-43, (2014). PMID: 24462206

6.Identification of Hsp90 as a species independent H5N1 avian influenza A virus PB2 interacting protein. Jirakanwisal K, Srisutthisamphan K, Thepparit C, Suptawiwat O, Auewarakul P, Paemanee A, Roytrakul S, Smith DR. Comp Immunol Microbiol Infect Dis 43, 28-35, (2015). PMID: 26616658

7.Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate. Sung N, Lee J, Kim JH, Chang C, Joachimiak A, Lee S, Tsai FT. Proc Natl Acad Sci U S A 113, 2952-7, (2016). PMID: 26929380

8.A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation. Echeverria PC, Briand PA, Picard D. Mol Cell Biol 36, 1310-21, (2016). PMID: 26884463

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