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First published online August 6, 2008

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Comings and goings in PML NBs

Promyelocytic leukemia nuclear bodies (PML NBs) – large multiprotein foci that exist within the nucleus of mammalian cells – are involved in diverse cellular processes that include apoptosis, the DNA-damage response and angiogenesis, but several key questions about the biochemical basis of their function remain. For instance, how dynamic is the protein composition of individual NBs, and what controls the association of component proteins? To shed light on these questions, Peter Hemmerich and colleagues (p. 2731) conduct a thorough analysis of the intranuclear dynamics of 11 component proteins of PML NBs, including the six splice variants of the PML protein (PML I-VI). Using FRAP, fluorescence correlation spectroscopy and computer modelling, the authors show that the PML isoforms exhibit markedly different residence times at PML NBs; in particular, PML V exchanges unusually slowly and might, the authors propose, act as a scaffold for other component proteins. The other proteins that are analysed – DAXX, BLM, HIPK2 and SP100 – exchange much more rapidly than the PML isoforms. Notably, conjugation by SUMO modulates the rate of exchange of PML isoforms and SP100. PML-NB composition is, therefore, highly plastic and subject to subtle regulation.

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Dynamics of component exchange at PML nuclear bodies

Stefanie Weidtkamp-Peters, Thorsten Lenser, Dmitri Negorev, Norman Gerstner, Thomas G. Hofmann, Georg Schwanitz, Christian Hoischen, Gerd Maul, Peter Dittrich, and Peter Hemmerich
JCS 2008 121: 2731-2743. [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?