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Biophys. J. BioFAST: First Published July 1, 2005. doi:10.1529/biophysj.105.062083
© 2005 by the Biophysical Society.

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MUSCLE AND CONTRACTILITY

Cofilin, Actin and Their Complex Observed In Vivo Using Fluorescence Resonance Energy Transfer

Deepak Chhabra 1* and Cristobal G dos Remedios 1

1 The University of Sydney

* To whom correspondence should be addressed. E-mail: dchhabra{at}anatomy.usyd.edu.au.

Submitted on February 28, 2005
Revised on March 28, 2005
Accepted on 20 June 2005


  Abstract
Actin is the principal component of microfilaments. Its assembly/disassembly is essential for cell motility, cytokinesis and a range of other functions. Recent evidence suggests that actin is present in the nucleus where it may be involved in the regulation of gene expression and that cofilin binds actin and can translocate into the nucleus during times of stress. In this report, we combine fluorescence resonance energy transfer (FRET) and confocal microscopy to analyze the interactions of cofilin and G-actin within the nucleus and cytoplasm. By measuring the rate of photobleaching of fluorescein-labeled actin in the presence and absence of Cy5-labeled cofilin, we determined that almost all G-actin in the nucleus is bound to cofilin, whereas approximately half is bound in the cytoplasm. Using FRET imaging techniques we observed that a significant proportion of fluorescein-labeled cofilin in both the nucleus and cytoplasm binds added TMR-labeled G-actin. Our data suggests there is significantly more cofilin-G-actin complex and less free cofilin in the nucleus than in the cytoplasm.

Key Words: Actin Binding Proteins, Confocal Microscopy, FRET, Forster resonance energy transfer, Photobleaching




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Copyright © 2005 by the Biophysical Society.