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MBC in Press, published online ahead of print June 20, 2007
Mol. Biol. Cell 10.1091/mbc.E07-01-0030

A more recent version of this article appeared on August 1, 2007 Originally published as MBC in Press, 10.1091/mbc.E07-01-0030 on June 13, 2007
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Submitted on January 16, 2007
Revised on April 19, 2007
Accepted on June 1, 2007

Dynein Light Chain Association Sequences Can Facilitate Nuclear Protein Import

Gregory W. Moseley,* Daniela Martino Roth,*{dagger} Michelle A. DeJesus,* Denisse L. Leyton,* Richard P. Filmer,* Colin W. Pouton,{dagger} and David A. Jans*

*Nuclear Signalling Laboratory, Department of Biochemistry and Molecular Biology, Monash University, Monash, Victoria 3800, Australia; {dagger}Department of Pharmaceutical Biology, Victorian College of Pharmacy, Monash University, Parkville, Victoria 3052, Australia

Monitoring Editor: Karsten Weis

Nuclear localization sequence (NLS)-dependent nuclear protein import is not conventionally held to require interaction with microtubules (MTs) or components of the MT motor, dynein. Here we report for the first time the role of sequences conferring association with dynein light chains (DLCs) in NLS-dependent nuclear accumulation of the rabies virus P-protein. We find that P-protein nuclear accumulation is significantly enhanced by its dynein light chain association sequence (DLC-AS), dependent on MT integrity and association with DLCs, and that P-protein-DLC complexes can associate with MT cytoskeletal structures. We also find that P-protein DLC-AS, as well as analogous sequences from other proteins, acts as an independent module which can confer enhancement of nuclear accumulation to proteins carrying the P-protein NLS, as well as several heterologous NLSs. Photobleaching experiments in live cells demonstrate that the MT-dependent enhancement of NLS-mediated nuclear accumulation by the P-protein DLC-AS involves an increased rate of nuclear import. This is the first report of DLC-AS enhancement of NLS function, identifying a novel mechanism regulating nuclear transport with relevance to viral and cellular protein biology. Importantly, this data indicates that DLC-AS represent versatile modules to enhance nuclear delivery with potential therapeutic application.

Address correspondence to: David A. Jans (david.jans{at}med.monash.edu.au)




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