2016
DOI: 10.1242/jcs.174995
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Translational control mediated by hnRNP K links NMHC IIA to erythroid enucleation

Abstract: Post-transcriptional regulation is crucial for structural and functional alterations in erythropoiesis. Enucleation of erythroid progenitors precedes reticulocyte release into circulation. In enucleated cells, reticulocyte 15-lipoxygenase (r15-LOX, also known as ALOX15) initiates mitochondria degradation. Regulation of r15-LOX mRNA translation by hnRNP K determines timely r15-LOX synthesis in terminal maturation. K562 cells induced for erythroid maturation recapitulate enucleation and mitochondria degradation.… Show more

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Cited by 15 publications
(9 citation statements)
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“…Y72 and Y458, respectively, are located at the KH1 and KH3 domains of hnRNPK. Phosphorylation of these residues affects their nucleic acid-binding affinity, reducing hnRNPK interaction with targets such as r15-LOX , TAK1 , UCP2 and NMHC IIA mRNA [27,28,46,66,67]. For example, r15-LOX mRNA translation activation is necessary for mature reticulocytes, while phosphorylation of Y458 in the KH3 domain diminishes the differentiation control element (DICE) binding activity of hnRNPK; consequently, its function as an inhibitor of r15-LOX mRNA translation is lost [30,64,68].…”
Section: Hnrnpk Phosphorylationmentioning
confidence: 99%
“…Y72 and Y458, respectively, are located at the KH1 and KH3 domains of hnRNPK. Phosphorylation of these residues affects their nucleic acid-binding affinity, reducing hnRNPK interaction with targets such as r15-LOX , TAK1 , UCP2 and NMHC IIA mRNA [27,28,46,66,67]. For example, r15-LOX mRNA translation activation is necessary for mature reticulocytes, while phosphorylation of Y458 in the KH3 domain diminishes the differentiation control element (DICE) binding activity of hnRNPK; consequently, its function as an inhibitor of r15-LOX mRNA translation is lost [30,64,68].…”
Section: Hnrnpk Phosphorylationmentioning
confidence: 99%
“…As multifunctional protein hnRNP K is associated with transcription activation (Moumen et al, 2005), pre-mRNA splicing (Expert-Bezancon et al, 2002), mRNA stability control (Skalweit et al, 2003) and regulation of mRNA translation (Ostareck et al, 1997, 2001; Collier et al, 1998; Naarmann et al, 2008, 2010; Naarmann-de Vries et al, 2016). HnRNP K functions are modulated by mRNA specific associated mRNP components (Ostareck-Lederer and Ostareck, 2012) and by post-translational modifications.…”
Section: Kh Domain Protein Hnrnp K Modulates Mrna Translationmentioning
confidence: 99%
“…In erythropoiesis, MYH9 is crucial for erythroid cell enucleation. This process was shown to depend on the activity of heterogeneous nuclear ribonucleoprotein K (hnRNP K), an RBP that inhibits translation of MYH9 mRNA [ 167 ]. It would be interesting to evaluate the effects of hnRNP K on MYH9 -dependent megakaryocyte maturation and platelet biogenesis, which has not been investigated so far.…”
Section: Post-transcriptional Gene Expression Control By Rbps and mentioning
confidence: 99%