![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
![[Contents]](/icons/banner/tocACT.gif){kind=icon}
|
|
|
|
|
||
Vol. 17, Issue 5, 2451-2464, May 2006
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226
Submitted December 28, 2005;
Revised February 13, 2006;
Accepted February 15, 2006
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 Caenorhabditis elegans and Drosophila melanogaster play an essential role in cell division; however, substrates that 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 (Barrier to Autointegration Factor). 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).
This article has been cited by other articles:
|
|
 |
|
  T. Haraguchi, T. Kojidani, T. Koujin, T. Shimi, H. Osakada, C. Mori, A. Yamamoto, and Y. Hiraoka Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly J. Cell Sci., August 1, 2008; 121(15): 2540 - 2554. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y.-C. J. Lin, J. Li, C. R. Irwin, H. Jenkins, L. DeLange, and D. H. Evans Vaccinia Virus DNA Ligase Recruits Cellular Topoisomerase II to Sites of Viral Replication and Assembly J. Virol., June 15, 2008; 82(12): 5922 - 5932. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T.-H. Kang, D.-Y. Park, Y. H. Choi, K.-J. Kim, H. S. Yoon, and K.-T. Kim Mitotic Histone H3 Phosphorylation by Vaccinia-Related Kinase 1 in Mammalian Cells Mol. Cell. Biol., December 15, 2007; 27(24): 8533 - 8546. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. M. Lancaster, C. F. Cullen, and H. Ohkura NHK-1 phosphorylates BAF to allow karyosome formation in the Drosophila oocyte nucleus J. Cell Biol., December 3, 2007; 179(5): 817 - 824. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F. S. De Silva, W. Lewis, P. Berglund, E. V. Koonin, and B. Moss Poxvirus DNA primase PNAS, November 20, 2007; 104(47): 18724 - 18729. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Blanco, C. Santos, and P. A. Lazo Vaccinia-Related Kinase 2 Modulates the Stress Response to Hypoxia Mediated by TAK1 Mol. Cell. Biol., October 15, 2007; 27(20): 7273 - 7283. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Margalit, E. Neufeld, N. Feinstein, K. L. Wilson, B. Podbilewicz, and Y. Gruenbaum Barrier to autointegration factor blocks premature cell fusion and maintains adult muscle integrity in C. elegans J. Cell Biol., August 9, 2007; 178(4): 661 - 673. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Haraguchi, T. Koujin, H. Osakada, T. Kojidani, C. Mori, H. Masuda, and Y. Hiraoka Nuclear localization of barrier-to-autointegration factor is correlated with progression of S phase in human cells J. Cell Sci., June 15, 2007; 120(12): 1967 - 1977. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L.-Y. Li, M.-Y. Liu, H.-M. Shih, C.-H. Tsai, and J.-Y. Chen Human cellular protein VRK2 interacts specifically with Epstein-Barr virus BHRF1, a homologue of Bcl-2, and enhances cell survival. J. Gen. Virol., October 1, 2006; 87(Pt 10): 2869 - 2878. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. R. Santos, S. Blanco, A. Sevilla, and P. A. Lazo Vaccinia Virus B1R Kinase Interacts with JIP1 and Modulates c-Jun-Dependent Signaling. J. Virol., August 1, 2006; 80(15): 7667 - 7675. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Valbuena, F. M. Vega, S. Blanco, and P. A. Lazo p53 Downregulates Its Activating Vaccinia-Related Kinase 1, Forming a New Autoregulatory Loop. Mol. Cell. Biol., July 1, 2006; 26(13): 4782 - 4793. [Abstract] [Full Text] [PDF]
|
|
