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XB-ART-13667
Mol Cell Biol 1999 Feb 01;192:1262-70. doi: 10.1128/MCB.19.2.1262.
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A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development.

Nielsen J , Christiansen J , Lykke-Andersen J , Johnsen AH , Wewer UM , Nielsen FC .


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Insulin-like growth factor II (IGF-II) is a major fetal growth factor. The IGF-II gene generates multiple mRNAs with different 5' untranslated regions (5' UTRs) that are translated in a differential manner during development. We have identified a human family of three IGF-II mRNA-binding proteins (IMPs) that exhibit multiple attachments to the 5' UTR from the translationally regulated IGF-II leader 3 mRNA but are unable to bind to the 5' UTR from the constitutively translated IGF-II leader 4 mRNA. IMPs contain the unique combination of two RNA recognition motifs and four hnRNP K homology domains and are homologous to the Xenopus Vera and chicken zipcode-binding proteins. IMP localizes to subcytoplasmic domains in a growth-dependent and cell-specific manner and causes a dose-dependent translational repression of IGF-II leader 3 -luciferase mRNA. Mouse IMPs are produced in a burst at embryonic day 12.5 followed by a decline towards birth, and, similar to IGF-II, IMPs are especially expressed in developing epithelia, muscle, and placenta in both mouse and human embryos. The results imply that cytoplasmic 5' UTR-binding proteins control IGF-II biosynthesis during late mammalian development.

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Species referenced: Xenopus
Genes referenced: brap hnrnpdl igf2bp3 ins

References [+] :
Allain, Structural basis of the RNA-binding specificity of human U1A protein. 1997, Pubmed