4.7 Article

Nuclear RNP complex assembly initiates cytoplasmic RNA localization

期刊

JOURNAL OF CELL BIOLOGY
卷 165, 期 2, 页码 203-211

出版社

ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200309145

关键词

RNA-binding protein; Vg1; VegT; Xenopus; oocyte

资金

  1. NICHD NIH HHS [R01 HD30699, R01 HD030699] Funding Source: Medline
  2. NIGMS NIH HHS [5-T32-GM07601, T32 GM007601, R01 GM071049] Funding Source: Medline

向作者/读者索取更多资源

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.

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