Protein phosphatase 2A regulatory subunit B56β modulates erythroid differentiation

Biochem Biophys Res Commun. 2016 Sep 23;478(3):1179-84. doi: 10.1016/j.bbrc.2016.08.090. Epub 2016 Aug 17.

Abstract

Anemia due to attenuated erythroid terminal differentiation is one of the most common hematological disorders occurring at all stages of life. We previously demonstrated that catalytic subunit α of protein phosphatase 2A (PP2Acα) modulates fetal liver erythropoiesis. However the corresponding PP2A regulatory subunit in this process remains unknown. In this study, we report that chemical inhibition of PP2A activity with okadaic acid impairs hemin-induced erythroid differentiation. Interestingly, B56 family member B56β is the only regulatory subunit whose expression is induced by both erythropoietin in fetal liver cells and hemin in erythroleukemia K562 cells. Finally, knockdown of B56β attenuates hemin-induced K562 erythroid differentiation. Collectively, our data identify B56β as the potential functional regulatory subunit of PP2A in erythroid differentiation, shedding light on new target for precise modulation of PP2A activity for treatment of anemia and related diseases.

Keywords: B56β; Erythroid differentiation; Erythropoiesis; PPP2R5B; Protein phosphatase 2A; Regulatory subunits.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Differentiation* / drug effects
  • Erythroid Cells / cytology*
  • Erythroid Cells / enzymology*
  • Gene Knockdown Techniques
  • Hemin / pharmacology
  • Humans
  • K562 Cells
  • Membrane Proteins / metabolism*
  • Mice, Inbred C57BL
  • Models, Biological
  • Okadaic Acid / pharmacology
  • Protein Phosphatase 2 / metabolism*

Substances

  • Membrane Proteins
  • Okadaic Acid
  • Hemin
  • PPP2R5B protein, human
  • Protein Phosphatase 2