Signaling to the DEAD box—Regulation of DEAD-box p68 RNA helicase by protein phosphorylations

Yang, Liuqing; Lin, Chunru; Liu, Zhi Ren

doi:10.1016/j.cellsig.2005.03.008

Cited by 21 publications

(18 citation statements)

References 60 publications

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“…p68 RNA helicase is a co-factor of Drosha in pri-miR processing [46] and is required for strand separation following dicer cleavage [47]; the ability of p68 to bind and unwind RNA is regulated by phosphorylation events [48,49].…”

Section: Regulation Of the Microrna Pathway By Cellular Signalingmentioning

confidence: 99%

Regulation of mammalian microRNA processing and function by cellular signaling and subcellular localization

Smalheiser

2008

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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For many microRNAs, in many normal tissues and in cancer cells, the cellular levels of mature microRNAs are not simply determined by transcription of microRNA genes. This mini-review will discuss how microRNA biogenesis and function can be regulated by various nuclear and cytoplasmic processing events, including emerging evidence that microRNA pathway components can be selectively regulated by control of their subcellular localization and by modifications that occur during dynamic cellular signaling. Finally, I will briefly summarize studies of microRNAs in synaptic fractions of adult mouse forebrain, which may serve as a model for other cell types as well.

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Section: Regulation Of the Microrna Pathway By Cellular Signalingmentioning

confidence: 99%

Regulation of mammalian microRNA processing and function by cellular signaling and subcellular localization

Smalheiser

2008

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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“…The MAP kinase phosphorylation target site on DDX5/p68 is crucial for its function in facilitating nuclear translocation of -catenin [114]. Further studies showed that phosphorylation of tyrosines in the Cterminal domain of DDX5/p68 abolish its RNA unwinding activity [114]. Therefore, there are clear indications that the different modifications of DDX5/p68 regulate its biological activity.…”

Section: Modifications Of Ddx Proteins Seem To Discriminate Between Tmentioning

confidence: 99%

“…DDX5/p68 becomes phosphorylated in response to PDGF stimulation [87] and the responsible kinase may be p38 MAP kinase. The MAP kinase phosphorylation target site on DDX5/p68 is crucial for its function in facilitating nuclear translocation of -catenin [114]. Further studies showed that phosphorylation of tyrosines in the Cterminal domain of DDX5/p68 abolish its RNA unwinding activity [114].…”

Section: Modifications Of Ddx Proteins Seem To Discriminate Between Tmentioning

confidence: 99%

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Cross Talk between Cellular Regulatory Networks Mediated by Shared Proteins

Dolde

Suter

2014

Advances in Biology

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Moonlighting proteins mediate cross talk between different pathways and cellular control networks. Sometimes, they even coordinate subsequent steps in the same pathway. For this Outlook paper we asked the question, which cellular processes employ multifunctional proteins (MFPs) and what makes them so attractive to cells and organisms. After reviewing their widespread occurrence, we will focus on higher eukaryotic model systems and on few examples that are linked to ongoing work in our laboratory. We will discuss the activities of transcription factor IIH (TFIIH), and its subcomplexes containing Xpd and Cdk7, and we will cover an aminoacyl-tRNA synthetase (LysRS) and DEAD box RNA helicases. Furthermore, we will analyze how cells are able to properly regulate the different biological activities of multifunctional proteins and which advantages such proteins offer to cells and organisms. Finally we also note that the proteins we discuss are linked to tumor formation or recruited by viruses that coopt the multifunctional protein for yet another purpose.

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“…In addition to the conserved motifs, there was an RGS-RGG motif identified as an RNA-binding domain of p68 [81]. Moreover, different phosphorylated residues may cause different decision on effects [82]. In conclusion, the main emphasis is placed on the topic on high correlation between phosphorylation of p68 and cancer development and progression, and more research is still required for the future diagnosis and therapy for cancer.…”

Section: Post-translational Modification Of P68 In Cancer Developmentmentioning

confidence: 99%

P68 RNA helicase as a molecular target for cancer therapy

Dai

Cao

Yang

et al. 2014

J Exp Clin Cancer Res

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The DEAD-box family of RNA helicase is known to be required in virtually all cellular processes involving RNA, and p68 is a prototypic one of the family. Reports have indicated that in addition to ATPase and RNA helicase ability, p68 can also function as a co-activator for transcription factors such as estrogen receptor alpha, tumor suppressor p53 and beta-catenin. More than that, post-translational modification of p68 including phosphorylation, acetylation, sumoylation, and ubiquitylation can regulate the coactivation effect. Furthermore, aberrant expression of p68 in cancers highlights that p68 plays an important role for tumorgenesis and development. In this review, we briefly introduce the function and modulation of p68 in cancer cells, and put forward envisagement about future study about p68.

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Signaling to the DEAD box—Regulation of DEAD-box p68 RNA helicase by protein phosphorylations

Cited by 21 publications

References 60 publications

Regulation of mammalian microRNA processing and function by cellular signaling and subcellular localization

Regulation of mammalian microRNA processing and function by cellular signaling and subcellular localization

Cross Talk between Cellular Regulatory Networks Mediated by Shared Proteins

P68 RNA helicase as a molecular target for cancer therapy

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