1989
DOI: 10.1073/pnas.86.10.3574
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A cytosolic protein binds to structural elements within the iron regulatory region of the transferrin receptor mRNA.

Abstract: The level of mRNA encoding the transferrin receptor (TfR) is regulated by iron, and this regulation is me-

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Cited by 218 publications
(118 citation statements)
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“…Modulation of translation by protein binding to the 5' or 3' UTR of mRNAs has been implicated as a general cellular regulatory mechanism for many genes including ferritin (22)(23)(24), transferrin receptor (9,25), and creatine kinase (26). Although the proteins and RNA elements of the ferritin and Prm-2 mRNAs differ, comparison of the RNA-protein complexes of ferritin and Prm-2 mRNAs reveals the strikingly similar interactions with cytoplasmic proteins (7,22,23).…”
Section: Methodsmentioning
confidence: 99%
“…Modulation of translation by protein binding to the 5' or 3' UTR of mRNAs has been implicated as a general cellular regulatory mechanism for many genes including ferritin (22)(23)(24), transferrin receptor (9,25), and creatine kinase (26). Although the proteins and RNA elements of the ferritin and Prm-2 mRNAs differ, comparison of the RNA-protein complexes of ferritin and Prm-2 mRNAs reveals the strikingly similar interactions with cytoplasmic proteins (7,22,23).…”
Section: Methodsmentioning
confidence: 99%
“…One mechanism used by cells to shut down expression of genes whose functions are no longer needed is to decompose their mRNA (2). Intrinsic signals for the decay of individual mRNA are often embedded in their 3Ј-UTR as cis-acting elements (3,4). Interactions of these elements with specific microRNA sequences or proteins provide fine-tune control over the half-lives of individual mRNAs (5)(6)(7).…”
mentioning
confidence: 99%
“…The spontaneous or diamide-induced formation of disulfide bonds between cysteines 437 and 503 or 437 and 506, in apo-IRF, as well as its alkylation by N-ethylmaleiniide, inhibit (Kuhn and Hentze, 1992;Leibold and Guo, 1992;Klausner et al, 1993). A soluble 98 kDa protein, iron regulatory factor (IRF), also called iron-responsive element-binding protein (IRE-BP), binds to specific RNA hairpin structures known as iron-responsive elements (IREs) (Leibold et al, 1988;Rouault et al, 1988;Koeller et al, 1989;Muillner et al, 1989). The IRE consists of a stable stem -10 nucleotides long, which is interrupted by an unpaired C positioned five nucleotides 5' of the loop.…”
mentioning
confidence: 99%