PKR forms a dimer

Stable Identifier
R-HSA-9833723
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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PKR (EIF2AK2) exists in a weak monomer/dimer equilibrium and, only when its catalytic domain is activated, acts as protein kinase. Dimerization-defective mutants of PKR cannot be activated by dsRNA. Apparently dsRNA and protein activators facilitate PKR dimerization which is the prerequisite for its autophosphorylation (Wu & Kaufman, 1997; Patel & Sen, 1995; Tian and Mathews 2001; Dey et al, 2005; Husain et al, 2015; reviewed by Cole, 2006).
Literature References
PubMed ID Title Journal Year
26488609 Regulation of PKR by RNA: formation of active and inactive dimers

Cole, JL, Husain, B, Hesler, S

Biochemistry 2015
17196820 Activation of PKR: an open and shut case?

Cole, JL

Trends Biochem Sci 2007
11134010 Functional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR

Tian, B, Mathews, MB

J Biol Chem 2001
16179259 Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition

Dey, M, Ozato, K, Cao, C, Dever, TE, Sicheri, F, Tamura, T, Dar, AC

Cell 2005
7545299 The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo

Patel, RC, Stanton, P, Williams, BR, Sen, GC, McMillan, NM

Proc Natl Acad Sci U S A 1995
8576179 Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR)

Kaufman, RJ, Wu, S

J Biol Chem 1996
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