Translational control mediated by hnRNP K links NMHC IIA to erythroid enucleation

Vries, Isabel S. Naarmann-de; Brendle, Annika; Bähr-Ivacevic, Tomi; Beneš, Vladimı́r; Ostareck, Dirk H.; Ostareck-Lederer, Antje

doi:10.1242/jcs.174995

Cited by 13 publications

(9 citation statements)

References 56 publications

(88 reference 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%

Post-translational modification control of RNA-binding protein hnRNPK function

Han

et al. 2019

Open Biol.

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Heterogeneous nuclear ribonucleoprotein K (hnRNPK), a ubiquitously occurring RNA-binding protein (RBP), can interact with numerous nucleic acids and various proteins and is involved in a number of cellular functions including transcription, translation, splicing, chromatin remodelling, etc. Through its abundant biological functions, hnRNPK has been implicated in cellular events including proliferation, differentiation, apoptosis, DNA damage repair and the stress and immune responses. Thus, it is critical to understand the mechanism of hnRNPK regulation and its downstream effects on cancer and other diseases. A number of recent studies have highlighted that several post-translational modifications (PTMs) possibly play an important role in modulating hnRNPK function. Phosphorylation is the most widely occurring PTM in hnRNPK. For example, in vivo analyses of sites such as S116 and S284 illustrate the purpose of PTM of hnRNPK in altering its subcellular localization and its ability to bind target nucleic acids or proteins. Other PTMs such as methylation, ubiquitination, sumoylation, glycosylation and proteolytic cleavage are increasingly implicated in the regulation of DNA repair, cellular stresses and tumour growth. In this review, we describe the PTMs that impact upon hnRNPK function on gene expression programmes and different disease states. This knowledge is key in allowing us to better understand the mechanism of hnRNPK regulation.

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Section: Hnrnpk Phosphorylationmentioning

confidence: 99%

Post-translational modification control of RNA-binding protein hnRNPK function

Han

et al. 2019

Open Biol.

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“…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%

RNA-Binding Proteins in the Control of LPS-Induced Macrophage Response

Ostareck

Ostareck-Lederer

2019

Front. Genet.

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Innate immune response is triggered by pathogen components, like lipopolysaccharides (LPS) of gram-negative bacteria. LPS initiates Toll-like receptor 4 (TLR4) signaling, which involves mitogen activated protein kinases (MAPK) and nuclear factor kappa B (NFκB) in different pathway branches and ultimately induces inflammatory cytokine and chemokine expression, macrophage migration and phagocytosis. Timely gene transcription and post-transcriptional control of gene expression confer the adequate synthesis of signaling molecules. As trans-acting factors RNA binding proteins (RBPs) contribute significantly to the surveillance of gene expression. RBPs are involved in the regulation of mRNA processing, localization, stability and translation. Thereby they enable rapid cellular responses to inflammatory mediators and facilitate a coordinated systemic immune response. Specific RBP binding to conserved sequence motifs in their target mRNAs is mediated by RNA binding domains, like Zink-finger domains, RNA recognition motifs (RRM), and hnRNP K homology domains (KH), often arranged in modular arrays. In this review, we focus on RBPs Tristetraprolin (TTP), human antigen R (HUR), T-cell intracellular antigen 1 related protein (TIAR), and heterogeneous ribonuclear protein K (hnRNP K) in LPS induced macrophages as primary responding immune cells. We discuss recent experiments employing RNA immunoprecipitation and microarray analysis (RIP-Chip) and newly developed individual-nucleotide resolution crosslinking and immunoprecipitation (iCLIP), photoactivatable ribonucleoside-enhanced crosslinking (PAR-iCLIP) and RNA sequencing techniques (RNA-Seq). The global mRNA interaction profile analysis of TTP, HUR, TIAR, and hnRNP K exhibited valuable information about the post-transcriptional control of inflammation related gene expression with a broad impact on intracellular signaling and temporal cytokine expression.

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“…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%

Post-Transcriptional Expression Control in Platelet Biogenesis and Function

Neu

Gutschner

Haemmerle

2020

IJMS

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Platelets are highly abundant cell fragments of the peripheral blood that originate from megakaryocytes. Beside their well-known role in wound healing and hemostasis, they are emerging mediators of the immune response and implicated in a variety of pathophysiological conditions including cancer. Despite their anucleate nature, they harbor a diverse set of RNAs, which are subject to an active sorting mechanism from megakaryocytes into proplatelets and affect platelet biogenesis and function. However, sorting mechanisms are poorly understood, but RNA-binding proteins (RBPs) have been suggested to play a crucial role. Moreover, RBPs may regulate RNA translation and decay following platelet activation. In concert with other regulators, including microRNAs, long non-coding and circular RNAs, RBPs control multiple steps of the platelet life cycle. In this review, we will highlight the different RNA species within platelets and their impact on megakaryopoiesis, platelet biogenesis and platelet function. Additionally, we will focus on the currently known concepts of post-transcriptional control mechanisms important for RNA fate within platelets with a special emphasis on RBPs.

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Translational control mediated by hnRNP K links NMHC IIA to erythroid enucleation

Cited by 13 publications

References 56 publications

Post-translational modification control of RNA-binding protein hnRNPK function

Post-translational modification control of RNA-binding protein hnRNPK function

RNA-Binding Proteins in the Control of LPS-Induced Macrophage Response

Post-Transcriptional Expression Control in Platelet Biogenesis and Function

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