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Published online 19 April 2004. doi:10.1083/jcb.200309145
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 2, 203-211
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Article

 Nuclear RNP complex assembly initiates cytoplasmic RNA localization

Tracy L. Kress, Young J. Yoon, and Kimberly L. Mowry

Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, RI 02912

Address correspondence to Kimberly L. Mowry, Box G-J2, Brown University, Providence, RI 02912. Tel.: (401) 863-3636. Fax: (401) 863-1201. email: kimberly_mowry{at}brown.edu

Cytoplasmic localization of mRNAs is a widespread mechanism for generating cell polarity and can provide the basis for patterning during embryonic development. A prominent example of this is localization of maternal mRNAs in Xenopus oocytes, a process requiring recognition of essential RNA sequences by protein components of the localization machinery. However, it is not yet clear how and when such protein factors associate with localized RNAs to carry out RNA transport. To trace the RNA–protein interactions that mediate RNA localization, we analyzed RNP complexes from the nucleus and cytoplasm. We find that an early step in the localization pathway is recognition of localized RNAs by specific RNA-binding proteins in the nucleus. After transport into the cytoplasm, the RNP complex is remodeled and additional transport factors are recruited. These results suggest that cytoplasmic RNA localization initiates in the nucleus and that binding of specific RNA-binding proteins in the nucleus may act to target RNAs to their appropriate destinations in the cytoplasm.

Key Words: RNA-binding protein; Vg1; VegT; Xenopus; oocyte

Abbreviation used in this paper: LE, localization element.


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