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First published online September 18, 2007
doi: 10.1242/10.1242/jcs.007492

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A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells

Wilfried Condemine^*, Yuki Takahashi^*, Morgane Le Bras and Hugues de Thé

CNRS/Université de Paris 7 UMR7151, Equipe labellisée par la Ligue Contre le Cancer, Hôpital St. Louis, 1 Av. C. Vellefaux 75475, Paris Cedex 10, France

Author for correspondence (e-mail: dethe{at}univ-paris-diderot.fr)

Accepted 12 July 2007

The promyelocytic leukemia (PML) tumour suppressor is the organiser of PML nuclear bodies, which are domains the precise functions of which are still disputed. We show that upon several types of stress, endogenous PML proteins form nucleolar caps and eventually engulf nucleolar components. Only two specific PML splice variants (PML-I and PML-IV) are efficiently targeted to the nucleolus and the abundant PML-I isoform is required for the targeting of endogenous PML proteins to this organelle. We identified a nucleolar targeting domain within the evolutionarily conserved C-terminus of PML-I. This domain contains a predicted exonuclease III fold essential for the targeting of the PML-I C-terminus to nucleolar fibrillar centres. Furthermore, spontaneous or oncogene retrieval-induced senescence is associated with the formation of very large PML nuclear bodies that initially contain nucleolar components. Later, poly-ubiquitin conjugates are found on the outer shell or within most of these senescence-associated PML bodies. Thus, unexpectedly, the scarcely studied PML-I isoform links PML bodies, nucleolus, senescence and proteolysis.

Key words: PML, Isoforms, Stress, Senescence, Proteasome, Nucleolus, Ubiquitin

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