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Molecular and Cellular Biology, January 2008, p. 678-686, Vol. 28, No. 2
0270-7306/08/$08.00+0 doi:10.1128/MCB.00999-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

James A. Gagnon, and
Kimberly L. Mowry*
Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Box G-L268, Providence, Rhode Island 02912
Received 6 June 2007/ Returned for modification 13 July 2007/ Accepted 1 November 2007
Transport of specific mRNAs to defined regions within the cell cytoplasm is a fundamental mechanism for regulating cell and developmental polarity. In the Xenopus oocyte, Vg1 RNA is transported to the vegetal cytoplasm, where localized expression of the encoded protein is critical for embryonic polarity. The Vg1 localization pathway is directed by interactions between key motifs within Vg1 RNA and protein factors recognizing those RNA sequences. We have investigated how RNA-protein interactions could be modulated to trigger distinct steps in the localization pathway and found that the Vg1 RNP is remodeled during cytoplasmic RNA transport. Our results implicate two RNA-binding proteins with key roles in Vg1 RNA localization, PTB/hnRNP I and Vg1RBP/vera, in this process. We show that PTB/hnRNP I is required for remodeling of the interaction between Vg1 RNA and Vg1RBP/vera. Critically, mutations that block this remodeling event also eliminate vegetal localization of the RNA, suggesting that RNP remodeling is required for localization.
Published ahead of print on 26 November 2007.
Present address: The Scripps Research Institute, Department of Cell Biology, CB163, La Jolla, CA 92037.
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