Abstract:
:Enucleation of erythroblasts during terminal differentiation is unique to mammals. Although erythroid enucleation has been extensively studied, only a few genes, including retinoblastoma protein (Rb), have been identified to regulate nuclear extrusion. It remains largely undefined by which signaling molecules, the extrinsic stimuli, such as erythropoietin (Epo), are transduced to induce enucleation. Here, we show that p38α, a mitogen-activated protein kinase (MAPK), is required for erythroid enucleation. In an ex vivo differentiation system that contains high Epo levels and mimics stress erythropoiesis, p38α is activated during erythroid differentiation. Loss of p38α completely blocks enucleation of primary erythroblasts. Moreover, p38α regulates erythroblast enucleation in a cell-autonomous manner in vivo during fetal and anemic stress erythropoiesis. Markedly, loss of p38α leads to downregulation of p21, and decreased activation of the p21 target Rb, both of which are important regulators of erythroblast enucleation. This study demonstrates that p38α is a key signaling molecule for erythroblast enucleation during stress erythropoiesis.
journal_name
Cell Resjournal_title
Cell researchauthors
Schultze SM,Mairhofer A,Li D,Cen J,Beug H,Wagner EF,Hui Ldoi
10.1038/cr.2011.159subject
Has Abstractpub_date
2012-03-01 00:00:00pages
539-50issue
3eissn
1001-0602issn
1748-7838pii
cr2011159journal_volume
22pub_type
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