PRMT1 arginine-methylates RUNX1

Stable Identifier
R-HSA-8934735
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Protein arginine methyltransferase 1 (PRMT1) methylates arginine residues R206 and R210 of RUNX1. Methylation of R206 and R210 inhibits binding of co-repressors to RUNX1, thus enhancing RUNX1 transcriptional activity (Zhao et al. 2008). In mice, arginine methylation seems to be dispensable for the function of RUNX1 in definitive hematopoiesis and steady-state platelet production, but is needed for the maintenance of the peripheral population of CD4+ T cells (Mizutani et al. 2015).

Literature References
PubMed ID Title Journal Year
26010396 Loss of RUNX1/AML1 arginine-methylation impairs peripheral T cell homeostasis

Mizutani, S, Yoshida, T, Zhao, X, Nimer, SD, Taniwaki, M, Okuda, T

Br. J. Haematol. 2015
18316480 Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity

Zhao, X, Jankovic, V, Gural, A, Huang, G, Pardanani, A, Menendez, S, Zhang, J, Dunne, R, Xiao, A, Erdjument-Bromage, H, Allis, CD, Tempst, P, Nimer, SD

Genes Dev. 2008
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein-arginine N-methyltransferase activity of RUNX1:CBFB:PRMT1 [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created