Calcium-dependent methylation by PRMT1 promotes erythroid differentiation through the p38α MAPK pathway

Mei Yin Liu, Wei Kai Hua, Yi Ying Chiou, Chi Ju Chen, Chao Ling Yao, Yi Ting Lai, Chao Hsiung Lin, Wey Jinq Lin

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Protein arginine methyltransferase 1 (PRMT1) stimulates erythroid differentiation, but the signaling events upstream are yet to be identified. Ca2+ plays crucial roles during erythroid differentiation. Here, we show that Ca2+ enhances methylation during induced erythroid differentiation and that Ca2+ directly upregulates the catalytic activity of recombinant PRMT1 by increasing Vmax toward the substrate heterogeneous nuclear ribonucleoprotein A2. We demonstrate that PRMT1 is essential and responsible for the effect of Ca2+ on differentiation. Depletion of Ca2+ suppresses PRMT1-mediated activation of p38α and p38α-stimulated differentiation. Furthermore, Ca2+ stimulates methylation of p38α by PRMT1. This study uncovers a novel regulatory mechanism for PRMT1 by Ca2+ and identifies the PRMT1/p38α axis as an intracellular mediator of Ca2+ signaling during erythroid differentiation.

Original languageEnglish
Pages (from-to)301-316
Number of pages16
JournalFEBS Letters
Issue number2
Publication statusPublished - 2020 Jan 1

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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