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MBC in Press, published online ahead of print February 22, 2006
Mol. Biol. Cell 10.1091/mbc.E05-12-1179

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Submitted on December 28, 2005
Revised on February 13, 2006
Accepted on February 15, 2006

The Vaccinia-related Kinases Phosphorylate the N Terminus of BAF, Regulating Its Interaction with DNA and Its Retention in the Nucleus

R. Jeremy Nichols,* Matthew S. Wiebe,* and Paula Traktman

Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226

Monitoring Editor: A. Gregory Matera

The vaccinia-related kinases (VRKs) comprise a branch of the casein kinase family whose members are characterized by homology to the vaccinia virus B1 kinase. The VRK orthologues encoded by C. elegans and D. melanogaster play an essential role in cell division; however, substrates which mediate this role have yet to be elucidated. VRK1 can complement the temperature-sensitivity of a vaccinia B1 mutant, implying that VRK1 and B1 have overlapping substrate specificity. Herein, we demonstrate that B1, VRK1 and VRK2 efficiently phosphorylate the extreme N' terminus of the BAF protein. BAF binds to both DNA and LEM domain-containing proteins of the inner nuclear membrane; in lower eukaryotes, BAF has been shown to play an important role during the reassembly of the nuclear envelope at the end of mitosis. We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of BAF with DNA and reduces its interaction with the LEM domain. Coexpression of VRK1 and GFP-BAF greatly diminishes the association of BAF with the nuclear chromatin/matrix and leads to its dispersal throughout the cell. Cumulatively, our data suggest that the VRKs may modulate the association of BAF with nuclear components, and hence play a role in maintaining appropriate nuclear architecture.

*These authors contributed equally to this work.

Address correspondence to: Paula Traktman (ptrakt{at}mcw.edu)




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