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XB-ART-12188
Mol Cell 1999 Sep 01;43:431-7. doi: 10.1016/s1097-2765(00)80345-7.
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A Xenopus protein related to hnRNP I has a role in cytoplasmic RNA localization.

Cote CA , Gautreau D , Denegre JM , Kress TL , Terry NA , Mowry KL .


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Cytoplasmic localization of mRNA molecules is a powerful mechanism for generating cell polarity. In vertebrates, one paradigm is localization of Vg1 RNA within the Xenopus oocyte, a process directed by recognition of a localization element within the Vg1 3' UTR. We show that specific base changes within the localization element abolish both localization in vivo and binding in vitro by a single protein, VgRBP60. VgRBP60 is homologous to a human hnRNP protein, hnRNP I, and combined immunolocalization and in situ hybridization demonstrate striking colocalization of hnRNP I and Vg1 RNA within the vegetal cytoplasm of the Xenopus oocyte. These results implicate a novel role in cytoplasmic RNA transport for this family of nuclear RNA-binding proteins.

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Species referenced: Xenopus
Genes referenced: gdf1 hnrnpc hnrnpdl hnrnpl ptbp1 s100a1
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