Human Interaction Network Ontology

Last uploaded: June 27, 2014
Preferred Name

PERK regulated gene expression
Synonyms
Definitions

Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31 Reviewed: Urano, F, 2010-04-30 Edited: May, B, Gopinathrao, G, 2008-11-19 19:22:37 Authored: May, B, 2009-06-02 00:51:49 PERK is a single-pass transmembrane protein located in the endoplasmic reticulum (ER) membrane such that the N-terminus of PERK is luminal and the C-terminus is cytosolic. PERK is maintained in an inactive form by interaction of its luminal domain with BiP, an ER chaperone. BiP also binds unfolded proteins and so BiP dissociates from PERK when unfolded proteins accumulate in the ER. Dissociated PERK monomers spontaneously form homodimers and the homodimeric form of PERK possesses kinase activity in its cytosolic C-terminal domain. The kinase specifically phosphorylates the translation factor eIF2alpha at Ser52, resulting in an arrest of translation. Thus translation of proteins targeted to the ER is downregulated. The translation arrest also causes depletion of Cyclin D1, a rapidly turned over protein. The depletion of Cyclin D1 in turn causes arrest of the cell cycle in G1 phase.

ID

http://purl.obolibrary.org/obo/HINO_0016044

comment

Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31

Reviewed: Urano, F, 2010-04-30

Edited: May, B, Gopinathrao, G, 2008-11-19 19:22:37

Authored: May, B, 2009-06-02 00:51:49

PERK is a single-pass transmembrane protein located in the endoplasmic reticulum (ER) membrane such that the N-terminus of PERK is luminal and the C-terminus is cytosolic. PERK is maintained in an inactive form by interaction of its luminal domain with BiP, an ER chaperone. BiP also binds unfolded proteins and so BiP dissociates from PERK when unfolded proteins accumulate in the ER. Dissociated PERK monomers spontaneously form homodimers and the homodimeric form of PERK possesses kinase activity in its cytosolic C-terminal domain. The kinase specifically phosphorylates the translation factor eIF2alpha at Ser52, resulting in an arrest of translation. Thus translation of proteins targeted to the ER is downregulated. The translation arrest also causes depletion of Cyclin D1, a rapidly turned over protein. The depletion of Cyclin D1 in turn causes arrest of the cell cycle in G1 phase.

definition source

Pubmed18048764

Reactome, http://www.reactome.org

Pubmed17956313

Pubmed18038217

Pubmed18436705

label

PERK regulated gene expression

located_in

http://purl.obolibrary.org/obo/NCBITaxon_9606

prefixIRI

HINO:0016044

prefLabel

PERK regulated gene expression

seeAlso

ReactomeREACT_18277

GENE ONTOLOGYGO:0006987

Reactome Database ID Release 43381042

subClassOf

http://purl.obolibrary.org/obo/INO_0000021

has_part

http://purl.obolibrary.org/obo/HINO_0008871

http://purl.obolibrary.org/obo/HINO_0016047

http://purl.obolibrary.org/obo/HINO_0014626

http://purl.obolibrary.org/obo/HINO_0008888

http://purl.obolibrary.org/obo/HINO_0008889

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