2002
DOI: 10.1006/jmbi.2001.5315
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Suppression of 15-lipoxygenase synthesis by hnRNP E1 is dependent on repetitive nature of LOX mRNA 3′-UTR control element DICE

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Cited by 58 publications
(56 citation statements)
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“…Only one repeat has been shown to be sufficient for binding of hnRNP E1, which does occur in a stoechiometric manner to the DICE. These findings implicate that at least two hnRNP molecules are required for translational regulation (Reimann et al, 2002).…”
Section: Regulation Of R15-lox Mrna Translation During Erythroid Cellmentioning
confidence: 84%
“…Only one repeat has been shown to be sufficient for binding of hnRNP E1, which does occur in a stoechiometric manner to the DICE. These findings implicate that at least two hnRNP molecules are required for translational regulation (Reimann et al, 2002).…”
Section: Regulation Of R15-lox Mrna Translation During Erythroid Cellmentioning
confidence: 84%
“…Precedents for regulation of translation at the step of subunit joining exist in several systems. For example, in early erythroid precursor cells, the mRNA encoding 15-lipoxygenase (r15-LOX) is translationally silenced at this step of translation initiation, dependent on a cytidine-rich 39 UTR element termed DICE (differentiation control element) and on two RNA-binding proteins: hnRNP K and hnRNP E1 (Ostareck et al 2001;Reimann et al 2002;Messias et al 2006). Phosphorylation of a specific tyrosine residue of hnRNP K by c-Src reduces its affinity for DICE, thus activating translation.…”
Section: Discussionmentioning
confidence: 99%
“…26 Indeed, a scan of the D4 sequence for sequences that may modify RNA stability and translational efficiency 27 identified hnRNP K and E binding sites, known as DICE, that are present as a tandem repeated sequence in the 15-lipoxygenase 3 0 untranslated region and suppress translation. 28,29 This identified consensus sequence is present in the region analyzed and includes sequences in the first repeat unit (a sequence). The observation that the single-stranded sense strand of the repeat 72 bp sequence, but not the antisense strand, could block the mobility shift of the nuclear factor (not shown) is consistent with this finding because KH domain proteins, like hnRNP K, can bind to single-stranded DNA with a similar specificity as to their RNA targets.…”
Section: O Schoots and Hhm Van Tolmentioning
confidence: 99%