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MBC in Press, published online ahead of print March 28, 2007
Mol. Biol. Cell 10.1091/mbc.E06-12-1075

A more recent version of this article appeared on June 1, 2007
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Submitted on December 5, 2006
Revised on February 26, 2007
Accepted on March 20, 2007

TRIM5{alpha} Cytoplasmic Bodies Are Highly Dynamic Structures

Edward M. Campbell,*{dagger} Mark P. Dodding,{dagger}{ddagger} Melvyn W. Yap,{ddagger} Xiaolu Wu,{sect} Sarah Gallois-Montbrun,|| Michael H. Malim,|| Jonathan P. Stoye,{ddagger} and Thomas J. Hope*

*Department of Cell and Molecular Biology, Northwestern University, Chicago, IL 60611-3008; {sect}Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612; {ddagger}Division of Virology, Medical Research Council National Institute for Medical Research, London, United Kingdom NW7 1AA; ||Department of Infectious Diseases, King’s College London School of Medicine, Guy’s Hospital, London, United Kingdom SE1 9RT

Monitoring Editor: Ralph Isberg

TRIM5{alpha} has recently been identified as a host restriction factor that has the ability to block infection by certain retroviruses in a species dependent manner. One interesting feature of this protein is that it is localized in distinct cytoplasmic clusters designated as cytoplasmic bodies. The potential role of these cytoplasmic bodies in TRIM5{alpha} function remains to be defined. By using fluorescent fusion proteins and live cell microcopy we studied the localization and dynamics of TRIM5{alpha} cytoplasmic bodies. This analysis reveals that cytoplasmic bodies are highly mobile, exhibiting both short saltatory movements and uni-directional long distance movements along the microtubule network. The morphology of the cytoplasmic bodies is also dynamic. Finally, photobleaching and photoactivation analysis reveals that the TRIM5{alpha} protein present in the cytoplasmic bodies is very dynamic, rapidly exchanging between cytoplasmic bodies and a more diffuse cytoplasmic population. Therefore, TRIM5{alpha} cytoplasmic bodies are dynamic structures more consistent with a role in function or regulation rather than protein aggregates or inclusion bodies that represent dead-end static structures.

{dagger}These authors contributed equally to this work.

Address correspondence to: Thomas J. Hope (thope{at}northwestern.edu)




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