SUMOylation of PKR

Stable Identifier
R-HSA-9834809
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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SUMO (Small Ubiquitin-like Modifier) proteins 1 and 2 (SUMO1, SUMO2) interact with protein kinase R (PKR, EIF2AK2) in both a covalent and non-covalent manner. SUMO E3 ligases can modify PKR on lysine residues 60, 150, and 440. Non-covalent interaction (complexation) of SUMO1 with PKR facilitates this covalent SUMOylation with subsequent autophosphorylation of PKR. However, as soon as lysine-162 is autophosphorylated, any complexation of SUMO1 is abandoned (de la Cruz-Herrera et al, 2014; de la Cruz-Herrera et al, 2017).
Literature References
PubMed ID Title Journal Year
25074923 Activation of the double-stranded RNA-dependent protein kinase PKR by small ubiquitin-like modifier (SUMO)

Campagna, M, Baz-Martínez, M, Lang, V, Garcia, MA, Marcos-Villar, L, de la Cruz-Herrera, CF, Vidal, A, Rivas, C, Gutiérrez, S, Rodriguez, MS, Esteban, M

J Biol Chem 2014
29070839 Phosphorylable tyrosine residue 162 in the double-stranded RNA-dependent kinase PKR modulates its interaction with SUMO

Baz-Martínez, M, Vidal, S, de la Cruz-Herrera, CF, Vidal, A, Rivas, C, Motiam, AE, Rodriguez, MS, Esteban, M, Collado, M

Sci Rep 2017
Participants
Participates
Catalyst Activity

SUMO ligase activity of unknown protein [cytosol]

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