In:
FEBS Letters, Wiley, Vol. 594, No. 2 ( 2020-01), p. 301-316
Abstract:
Protein arginine methyltransferase 1 (PRMT1) stimulates erythroid differentiation, but the signaling events upstream are yet to be identified. Ca 2+ plays crucial roles during erythroid differentiation. Here, we show that Ca 2+ enhances methylation during induced erythroid differentiation and that Ca 2+ directly upregulates the catalytic activity of recombinant PRMT1 by increasing V max toward the substrate heterogeneous nuclear ribonucleoprotein A2. We demonstrate that PRMT1 is essential and responsible for the effect of Ca 2+ on differentiation. Depletion of Ca 2+ suppresses PRMT1‐mediated activation of p38α and p38α‐stimulated differentiation. Furthermore, Ca 2+ stimulates methylation of p38α by PRMT1. This study uncovers a novel regulatory mechanism for PRMT1 by Ca 2+ and identifies the PRMT1/p38α axis as an intracellular mediator of Ca 2+ signaling during erythroid differentiation.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1002/1873-3468.13614
Language:
English
Publisher:
Wiley
Publication Date:
2020
detail.hit.zdb_id:
1460391-3
SSG:
12
