Show simple item record

dc.contributor.authorChu, Jenniferen_US
dc.contributor.authorCencic, Reginaen_US
dc.contributor.authorWang, Wenyuen_US
dc.contributor.authorPorco, John A.en_US
dc.contributor.authorPelletier, Jerryen_US
dc.coverage.spatialUnited Statesen_US
dc.date2015-10-29
dc.date.accessioned2018-01-30T16:42:37Z
dc.date.available2018-01-30T16:42:37Z
dc.date.issued2016-01
dc.identifierhttps://www.ncbi.nlm.nih.gov/pubmed/26586722
dc.identifier.citationJennifer Chu, Regina Cencic, Wenyu Wang, John A Porco, Jerry Pelletier. 2016. "Translation Inhibition by Rocaglates Is Independent of eIF4E Phosphorylation Status.." Mol Cancer Ther, Volume 15, Issue 1, pp. 136 - 141.
dc.identifier.issn1538-8514
dc.identifier.urihttps://hdl.handle.net/2144/26492
dc.description.abstractRocaglates are natural products that inhibit protein synthesis in eukaryotes and exhibit antineoplastic activity. In vitro biochemical assays, affinity chromatography experiments coupled with mass spectrometry analysis, and in vivo genetic screens have identified eukaryotic initiation factor (eIF) 4A as a direct molecular target of rocaglates. eIF4A is the RNA helicase subunit of eIF4F, a complex that mediates cap-dependent ribosome recruitment to mRNA templates. The eIF4F complex has been implicated in tumor initiation and maintenance through elevated levels or increased phosphorylation status of its cap-binding subunit, eIF4E, thus furthering the interest toward developing rocaglates as antineoplastic agents. Recent experiments have indicated that rocaglates also interact with prohibitins 1 and 2, proteins implicated in c-Raf-MEK-ERK signaling. Because increased ERK signaling stimulates eIF4E phosphorylation status, rocaglates are also expected to inhibit eIF4E phosphorylation status, a point that has not been thoroughly investigated. It is currently unknown whether the effects on translation observed with rocaglates are solely through eIF4A inhibition or also a feature of blocking eIF4E phosphorylation. Here, we show that rocaglates inhibit translation through an eIF4E phosphorylation-independent mechanism.en_US
dc.description.sponsorshipP50 GM067041 - NIGMS NIH HHS; R01 GM073855 - NIGMS NIH HHS; GM-067041 - NIGMS NIH HHS; MOP-106530 - Canadian Institutes of Health Researchen_US
dc.format.extent136 - 141en_US
dc.languageeng
dc.relation.ispartofMol Cancer Ther
dc.subjectScience & technologyen_US
dc.subjectLife sciences & biomedicineen_US
dc.subjectOncologyen_US
dc.subjectProtein synthesisen_US
dc.subjectFactor 4Aen_US
dc.subjectSilvestrolen_US
dc.subjectRocaglamidesen_US
dc.subjectTumorigenesisen_US
dc.subjectAnimalsen_US
dc.subjectAntineoplastic agentsen_US
dc.subjectBenzofuransen_US
dc.subjectBiological productsen_US
dc.subjectCell lineen_US
dc.subjectCyclopentanesen_US
dc.subjectEukaryotic Initiation Factor-4Een_US
dc.subjectHumansen_US
dc.subjectPhosphorylationen_US
dc.subjectProtein biosynthesisen_US
dc.subjectSignal transductionen_US
dc.subjectOncology and carcinogenesisen_US
dc.subjectPharmacology and pharmaceutical sciencesen_US
dc.subjectOncology & carcinogenesisen_US
dc.titleTranslation inhibition by rocaglates is independent of eIF4E phosphorylation statusen_US
dc.typeArticleen_US
dc.identifier.doi10.1158/1535-7163.MCT-15-0409
pubs.elements-sourcepubmeden_US
pubs.notesEmbargo: Not knownen_US
pubs.organisational-groupBoston Universityen_US
pubs.organisational-groupBoston University, College of Arts & Sciencesen_US
pubs.organisational-groupBoston University, College of Arts & Sciences, Department of Chemistryen_US
pubs.publication-statusPublisheden_US


This item appears in the following Collection(s)

Show simple item record