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First published online September 18, 2007

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Stressed PML goes nucleolar

PML bodies are small nuclear structures that contain promyelocytic leukaemia (PML) protein, a member of the RING finger, B-box, coiled-coil (RBCC) family. They are implicated in many nuclear processes, but the precise function of the PML protein remains unclear. Now, Hugues de Thé and colleagues report that the poorly understood isoform PML-I targets PML proteins to the nucleolus in stressed and senescent cells (see p. 3219). The authors show that, after genotoxic stress, endogenous PML proteins move to the nucleolus. By expressing individual PML isoforms in Pml^–/– fibroblasts, they show that only the evolutionarily conserved PML splice variants PML-I and PML-IV are efficiently targeted to the nucleolus after stress. They also demonstrate that knocking down PML-I by RNAi inhibits stress-induced nucleolar targeting of endogenous PML proteins and identify a nucleolar targeting domain within the C-terminus of PML-I. Finally, they report that large PML bodies, which initially contain nucleolar components but subsequently accumulate poly-ubiquitin conjugates, form in senescent cells. Thus, the C-terminal nucleolar targeting domain of PML-1 is part of a novel mechanism connecting PML bodies, the nucleolus, senescence and proteolysis.

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Related articles in JCS:

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
JCS 2007 120: 3219-3227. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?