Human Interaction Network Ontology

Last uploaded: June 27, 2014
Preferred Name

TLR folding by chaperones GP96 and CNPY3
Synonyms
Definitions

has a Stoichiometric coefficient of 2 Edited: Shamovsky, V, 2012-02-19 Reviewed: Leifer, CA, Rose II, WA, 2012-02-28 GP96 (also known as GRP94, HSP90b1), a paralogue of HSP90 in the endoplasmic reticulum, acts as a chaperone for some integrines and Toll-like receptors. Macrophages or B-cells from gp96 knockout mice have abrogated function of TLR2, 4, 5, 7 and 9, but not TLR3 (Yang Y et al 2007, Liu B and Li Z 2008, Staron M et al 2010). GP96 interacts with TLRs and integrines via its C-terminal hydrophobic domain, formed by residues 652-678 (Wu S et al 2012). GP96 functions as a V-shaped dimer in ATP-dependent manner, however it remains unclear how ATP hydrolysis-dependent conformational changes of GP96 are regulated (Li Z and Srivastava PK 1993).<p>GP96 forms a complex with co-chaperone CNPY3, also known as PRAT4A. GP96-CNPY3 promotes the proper post-translational ectodomain folding of TLRs, but not TLR3 (Liu B et al 2010). Reviewed: Gillespie, ME, 2012-02-09 Authored: Shamovsky, V, 2011-10-19

ID

http://purl.obolibrary.org/obo/HINO_0018093

comment

has a Stoichiometric coefficient of 2

Edited: Shamovsky, V, 2012-02-19

Reviewed: Leifer, CA, Rose II, WA, 2012-02-28

GP96 (also known as GRP94, HSP90b1), a paralogue of HSP90 in the endoplasmic reticulum, acts as a chaperone for some integrines and Toll-like receptors. Macrophages or B-cells from gp96 knockout mice have abrogated function of TLR2, 4, 5, 7 and 9, but not TLR3 (Yang Y et al 2007, Liu B and Li Z 2008, Staron M et al 2010). GP96 interacts with TLRs and integrines via its C-terminal hydrophobic domain, formed by residues 652-678 (Wu S et al 2012). GP96 functions as a V-shaped dimer in ATP-dependent manner, however it remains unclear how ATP hydrolysis-dependent conformational changes of GP96 are regulated (Li Z and Srivastava PK 1993).

GP96 forms a complex with co-chaperone CNPY3, also known as PRAT4A. GP96-CNPY3 promotes the proper post-translational ectodomain folding of TLRs, but not TLR3 (Liu B et al 2010).

Reviewed: Gillespie, ME, 2012-02-09

Authored: Shamovsky, V, 2011-10-19

definition source

Pubmed22223641

Pubmed18509083

Reactome, http://www.reactome.org

Pubmed8344253

Pubmed19965672

Pubmed20865800

Pubmed17275357

has input

http://purl.obolibrary.org/obo/UniProt_Q9BT09

http://purl.obolibrary.org/obo/HINO_0004183

http://purl.obolibrary.org/obo/HINO_0005253

http://purl.obolibrary.org/obo/CHEBI_15422

has output

http://purl.obolibrary.org/obo/HINO_0005251

label

TLR folding by chaperones GP96 and CNPY3

prefixIRI

HINO:0018093

prefLabel

TLR folding by chaperones GP96 and CNPY3

seeAlso

ReactomeREACT_118729

Reactome Database ID Release 431678923

subClassOf

http://purl.obolibrary.org/obo/INO_0000040

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