Abstract：
:PML nuclear bodies (NBs) are involved in the regulation of key nuclear pathways but their biochemical function in nuclear metabolism is unknown. In this study PML NB assembly dynamics were assessed by live cell imaging and mathematic modeling of its major component parts. We show that all six nuclear PML isoforms exhibit individual exchange rates at NBs and identify PML V as a scaffold subunit. SP100 exchanges at least five times faster at NBs than PML proteins. Turnover dynamics of PML and SP100 at NBs is modulated by SUMOylation. Exchange is not temperature-dependent but depletion of cellular ATP levels induces protein immobilization at NBs. The PML-RARalpha oncogene exhibits a strong NB retention effect on wild-type PML proteins. HIPK2 requires an active kinase for PML NB targeting and elevated levels of PML IV increase its residence time. DAXX and BLM turn over rapidly and completely at PML NBs within seconds. These findings provide a kinetics model for factor exchange at PML NBs and highlight potential mechanisms to regulate intranuclear trafficking of specific factors at these domains.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Weidtkamp-Peters S,Lenser T,Negorev D,Gerstner N,Hofmann TG,Schwanitz G,Hoischen C,Maul G,Dittrich P,Hemmerich Pdoi
10.1242/jcs.031922subject
Has Abstractpub_date
2008-08-15 00:00:00pages
2731-43issue
Pt 16eissn
0021-9533issn
1477-9137pii
jcs.031922journal_volume
121pub_type
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