PGAM5 dodecamer dephosphorylates p-S336-ME1

Stable Identifier
R-HSA-9861725
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Serine/threonine-protein phosphatase PGAM5 (aka phosphoglycerate mutase family member 5), localized on the outer mitochondrial membrane, dephosphorylates cytosolic p-S336-ME1, restoring its catalytic activity (Lo & Hannink, 2008; Zhu et al., 2020). PGAM5 forms tubular filaments composed of stacked dodecameric rings which are essential for PGAM5 catalysis (Ruiz et al., 2019).
Literature References
PubMed ID Title Journal Year
18387606 PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

Hannink, M, Lo, SC

Exp Cell Res 2008
30705304 Functional role of PGAM5 multimeric assemblies and their polymerization into filaments

Jura, N, Frost, A, Ingaramo, M, Agnew, C, Ruiz, K, Herrera, C, Thaker, TM, Miller-Vedam, L, Toso, D, Trenker, R

Nat Commun 2019
31735643 Dynamic Regulation of ME1 Phosphorylation and Acetylation Affects Lipid Metabolism and Colorectal Tumorigenesis

Lin, X, Li, Y, Zhu, Y, Gu, L, Prochownik, EV, Fan, C, Zhao, Q, Zhou, F, Lu, B, Cui, K, Liu, C

Mol Cell 2020
Participants
Participates
Catalyst Activity

protein serine/threonine phosphatase activity of PGAM5 dodecamer [mitochondrial outer membrane]

Orthologous Events
Cross References
RHEA
Authored
Reviewed
Created
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