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MBC in Press, published online ahead of print October 15, 2008
Mol. Biol. Cell 10.1091/mbc.E08-09-0904

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Submitted on September 3, 2008
Revised on September 30, 2008
Accepted on October 6, 2008

Nucleocytoplasmic Traffic of CPEB1 and Accumulation in Crm1-Nucleolar-Bodies

Michèle Ernoult-Lange,* Ania Wilczynska,*{dagger}{ddagger} Maryannick Harper,* Christelle Aigueperse,* François Dautry,* Michel Kress,* and Dominique Weil*

*CNRS FRE2937, Institut André Lwoff, 94801 Villejuif Cedex, France; {dagger}Department of Molecular Biology, Warsaw Cancer Center, 02-781 Warszawa, Poland

Monitoring Editor: Marvin Wickens

The translational regulator CPEB1 plays a major role in the control of maternal mRNA in oocytes, as well as of subsynaptic mRNAs in neurons. Although mainly cytoplasmic, we found that CPEB1 protein is continuously shuttling between nucleus and cytoplasm. Its export is controlled by two redundant NES motifs dependent on the nuclear export receptor Crm1. In the nucleus, CPEB1 accumulates in a few foci most often associated to nucleoli. These foci are different from previously identified nuclear bodies. They contain Crm1 and were called CNoBs, for Crm1-Nucleolar-Bodies. CNoBs depend on RNA polymerase I activity, indicating a role in ribosome biogenesis. However, although they form in the nucleolus, they never migrate to nuclear envelope, precluding a role as a mediator for ribosome export. They could rather constitute a platform providing factors for ribosome assembly or export. The behavior of CPEB1 in CNoBs raises the possibility that it is involved in ribosome biogenesis.

{ddagger}Present address: Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.

Address correspondence to: Dominique Weil (weil{at}vjf.cnrs.fr)




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