Protein Arginine Methyltransferase 1 Interacts with and Activates p38α to Facilitate Erythroid Differentiation
Figure 5
PRMT1 physically interacted with and methylated p38α.
(A) An anti-p38α specific antibody was used to immunoprecipitate p38α from K562 cell lysates. PRMT1 was associated with the precipitates (upper panel). In addition, p38α was co-immunoprecipitated when an anti-PRMT1 specific antibody was used (lower panel). Mouse IgG was used as a negative control. (B) The recombinant His-p38α protein was methylated in vitro by GST-PRMT1 in a time-dependent manner (30–60 min) as detected by fluorography. No methyl incorporation was observed in the absence of either the substrate (p38α) or the enzyme (PRMT1). All results shown are representative of three separate experiments.
