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Originally published as MBC in Press, 10.1091/mbc.E08-09-0904 on October 15, 2008

Vol. 20, Issue 1, 176-187, January 1, 2009

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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; and {dagger}Department of Molecular Biology, Warsaw Cancer Center, 02-781 Warszawa, Poland

Submitted September 3, 2008; Revised September 30, 2008; Accepted October 6, 2008
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 with nucleoli. These foci are different from previously identified nuclear bodies. They contain Crm1 and were called Crm1 nucleolar bodies (CNoBs). CNoBs depend on RNA polymerase I activity, indicating a role in ribosome biogenesis. However, although they form in the nucleolus, they never migrate to the 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.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-09-0904) on October 15, 2008.

{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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