DEAD box RNA helicase functions in cancer

Fuller-Pace, Frances V.

doi:10.4161/rna.23312

Cited by 161 publications

(158 citation statements)

References 122 publications

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“…In lung cells, the activation of p21 by p53 is synergistically enhanced by the DDX3 protein-a member of the DEAD box family of proteins that contains the RNA helicase domain, the expression of which is activated by p53 (Wu et al 2011). DEAD box RNA helicases play a role in RNA metabolism by coupling transcription, slicing, RNA export and translation (Wu et al 2011;Fuller-Pace 2013). It is believed that DDX3 is involved in the regulation of the cell cycle and apoptosis and thus has an importance in cancer development (Lai et al 2010;Fuller-Pace 2013).…”

Section: Possible Molecular Mechanisms Of Hpv Induces Lung Carcinogenmentioning

confidence: 99%

“…DEAD box RNA helicases play a role in RNA metabolism by coupling transcription, slicing, RNA export and translation (Wu et al 2011;Fuller-Pace 2013). It is believed that DDX3 is involved in the regulation of the cell cycle and apoptosis and thus has an importance in cancer development (Lai et al 2010;Fuller-Pace 2013). In cell culture, it was observed that DDX3 facilitates translation initiation of cyclin E1mRNA, whose function is to activate genes involved in the S-phase entry and DNA replication by phosphorylation of pRb and subsequent release of the transcription factor E2F (Lai et al 2010;Fig.…”

Section: Possible Molecular Mechanisms Of Hpv Induces Lung Carcinogenmentioning

confidence: 99%

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Human papillomavirus and lung cancinogenesis: an overview

Freitas

Gurgel

Lima

et al. 2016

J Cancer Res Clin Oncol

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Lung cancer is the most common cause of cancer deaths worldwide. Although tobacco smoking is considered to be the main risk factor and the most well-established risk factor for lung cancer, a number of patients who do not smoke have developed this disease. This number varies between 15 % to over one-half of lung cancer cases, and the deaths from lung cancer in non-smokers are increasing every year. There are many other agents that are thought to be etiological, including diesel exhaust exposure, metals, radiation, radon, hormonal factors, cooking oil, air pollution and infectious diseases, such as human papillomavirus (HPV). Studies in various parts of the world have detected HPV DNA at different rates in lung tumors. However, the role of HPV in lung cancer is still unclear. Thus, in this review, we investigated some molecular mechanisms of HPV protein activity in host cells, the entry of HPV into lung tissue and the possible route used by the virus to reach the lung cells.

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Section: Possible Molecular Mechanisms Of Hpv Induces Lung Carcinogenmentioning

confidence: 99%

Section: Possible Molecular Mechanisms Of Hpv Induces Lung Carcinogenmentioning

confidence: 99%

Human papillomavirus and lung cancinogenesis: an overview

Freitas

Gurgel

Lima

et al. 2016

J Cancer Res Clin Oncol

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“…Since p68 is ubiquitously expressed in human tissues and plays a multifunctional role in a number of the cellular processes, many experimental results revealed examples of diseases concerned with p68, including obesity [38], Down syndrome [39], myotonic dystrophies [40] and especially cancer [5]. Over the past few decades, abnormal expression of p68 has been detected in many cancers, such as colon cancer [41], breast cancer [42], lung cancer [43], cutaneous squamous cell carcinoma [44], leukemia [45] and so on ( Table 1).…”

Section: Abnormal Expression Of P68 In Cancermentioning

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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“…There is also evidence supporting a role of DDX3 RNA helicase in promoting the translation initiation of a specific subset of mRNAs that include complex secondary structure in their 5= untranslated regions (5= UTRs) (27,(31)(32)(33). DDX3 is also implicated in cancer; however, as for its role in protein translation, the results are mixed, suggesting both oncogenic and tumor suppressor functions (25,(33)(34)(35)(36)(37)(38)(39)(40)(41)(42).…”

mentioning

confidence: 91%

“…Studies concerning the role of DDX3 in cancer have shown ambiguous results, suggesting both oncogenic and tumor suppressor functions, depending on the cancer type (23,34). This dual role of DDX3 could be related to its precise function in regulation of translation, which might be differentially modulated in different types of cells and under different conditions (e.g., stress conditions).…”

Section: Figmentioning

confidence: 99%

Ezrin Binds to DEAD-Box RNA Helicase DDX3 and Regulates Its Function and Protein Level

Çelik

Sajwan

Selvanathan

et al. 2015

Molecular and Cellular Biology

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Ezrin is a key regulator of cancer metastasis that links the extracellular matrix to the actin cytoskeleton and regulates cell morphology and motility. We discovered a small-molecule inhibitor, NSC305787, that directly binds to ezrin and inhibits its function. In this study, we used a nano-liquid chromatography-tandem mass spectrometry (nano-LC-MS-MS)-based proteomic approach to identify ezrin-interacting proteins that are competed away by NSC305787. A large number of the proteins that interact with ezrin were implicated in protein translation and stress granule dynamics. We validated direct interaction between ezrin and the RNA helicase DDX3, and NSC305787 blocked this interaction. Downregulation or long-term pharmacological inhibition of ezrin led to reduced DDX3 protein levels without changes in DDX3 mRNA. Ectopic overexpression of ezrin in low-ezrin-expressing osteosarcoma cells caused a notable increase in DDX3 protein levels. Ezrin inhibited the RNA helicase activity of DDX3 but increased its ATPase activity. Our data suggest that ezrin controls the translation of mRNAs preferentially with a structured 5= untranslated region, at least in part, by sustaining the protein level of DDX3 and/or regulating its function. Therefore, our findings suggest a novel function for ezrin in regulation of gene translation that is distinct from its canonical role as a cytoskeletal scaffold at the cell membrane. Ezrin is a prototype member of the ERM (ezrin-radixin-moesin) family of proteins that functions as a scaffold between the plasma membrane and the underlying cortical actin cytoskeleton (1, 2). Ezrin regulates cytoskeletal dynamics in response to both internal and external stimuli through its intracellular localization and protein binding activities; thus, it plays an important role in the maintenance of cell shape, cell polarity, adhesion, and movement (3). All members of the ERM family are characterized by the presence of a shared FERM domain at the amino terminus, which can bind to transmembrane proteins, including CD43, CD44, CD95, ICAMs, syndecan 2, EBP50/NHERF1, and E3KARP/NHERF2. The carboxy termini of ERM proteins contain an F-actin binding domain, which both regulates intramolecular interactions with amino-terminal FERM domains and promotes F-actin organization. The pleiotropic functions of ezrin in a wide range of cellular processes can be explained through its association with numerous proteins with diverse functions (4). Several lines of evidence have indicated that ezrin can oscillate between various "open/active" and "closed/dormant" states, which are regulated by self-association of N-terminal and Cterminal regions. Head-to-tail folding of the molecule likely masks the respective protein binding sites and leads to the localization of ezrin in the cytoplasm in its monomeric form. The conformational switch to an open state requires direct interaction with the plasma membrane phospholipid phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2 ] and phosphorylation of a conserved threonine (T567) located in the ...

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DEAD box RNA helicase functions in cancer

Cited by 161 publications

References 122 publications

Human papillomavirus and lung cancinogenesis: an overview

Human papillomavirus and lung cancinogenesis: an overview

P68 RNA helicase as a molecular target for cancer therapy

Ezrin Binds to DEAD-Box RNA Helicase DDX3 and Regulates Its Function and Protein Level

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