p-PKR dimer phosphorylates PPP2R5A

Stable Identifier
R-HSA-9836664
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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PPP2R5A, as a subunit of the phosphatase PP2A complex, can regulate the cellular location, substrate specification, and protein phosphatase function of PP2A. Protein kinase R (PKR, EIF2AK2) phosphorylates PPP2R5A at S28, which results in mitochondrial localization of PPP2R5A and activation of the PP2A holoenzyme. In contrast, silencing PKR significantly suppressed the activity of PP2A. PP2A activation supports apoptotic processes that likely include inactivation of BCL2 by dephosphorylation (Xu & Williams, 2000; Ruvolo et al, 2008; Yang et al, 2010; reviewed by Mao et al, 2018).
Literature References
PubMed ID Title Journal Year
29175459 PPP2R5A: A multirole protein phosphatase subunit in regulating cancer development

Su, C, Sun, B, Lin, X, Mao, Z, Liu, C

Cancer Lett 2018
10866685 The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKR

Williams, BR, Xu, Z

Mol Cell Biol 2000
18957415 PKR regulates B56(alpha)-mediated BCL2 phosphatase activity in acute lymphoblastic leukemia-derived REH cells

Ruvolo, VR, Schuster, TF, Ruvolo, PP, Karanjeet, KB, Martelli, AM, Kurinna, SM, McCubrey, JA

J Biol Chem 2008
20685959 The double-stranded RNA-dependent protein kinase differentially regulates insulin receptor substrates 1 and 2 in HepG2 cells

Opperman, MJ, Yang, X, Chan, C, Nath, A

Mol Biol Cell 2010
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Catalyst Activity

protein kinase activity of p-EIF2AK2 dimer [cytosol]

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