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Published 13 February 2006. doi:10.1083/jcb.200507101
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 4, 541-552
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Article

 Nucleoplasmic ß-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations

Darin McDonald1, Gustavo Carrero2, Christi Andrin1, Gerda de Vries2, and Michael J. Hendzel1

1 Department of Oncology and 2 Department of Mathematical and Statistical Sciences, University of Alberta, Edmonton, Alberta, Canada T6G 1Z2

Correspondence to Michael J. Hendzel: michaelh{at}cancerboard.ab.ca

ß-Actin, once thought to be an exclusively cytoplasmic protein, is now known to have important functions within the nucleus. Nuclear ß-actin associates with and functions in chromatin remodeling complexes, ribonucleic acid polymerase complexes, and at least some ribonucleoproteins. Proteins involved in regulating actin polymerization are also found in the interphase nucleus. We define the dynamic properties of nuclear actin molecules using fluorescence recovery after photobleaching. Our results indicate that actin and actin-containing complexes are reduced in their mobility through the nucleoplasm diffusing at ~0.5 µm2 s–1. We also observed that ~20% of the total nuclear actin pool has properties of polymeric actin that turns over rapidly. This pool could be detected in endogenous nuclear actin by using fluorescent polymeric actin binding proteins and was sensitive to drugs that alter actin polymerization. Our results validate previous reports of polymeric forms of nuclear actin observed in fixed specimens and reveal that these polymeric forms are very dynamic.

Abbreviations used in this paper: DRB, 5,6-dichloro-1-ß-D-ribofuranosylbenzimidazole; FCS, fluorescence correlation spectroscopy; FRAP, fluorescence recovery after photobleaching; mRNP, messenger RNP.


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