QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 17, Issue 4, 1711-1722, April 2006

This Article Full Text Full Text (PDF) Supplemental Material All Versions of this Article: E05-11-1063v1 17/4/1711    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Moorefield, K. S. Articles by Horowitz, J. M. Search for Related Content PubMed PubMed Citation Articles by Moorefield, K. S. Articles by Horowitz, J. M.

Sp2 Localizes to Subnuclear Foci Associated with the Nuclear Matrix

K. Scott Moorefield ^*, Haifeng Yin ^*, Teresa D. Nichols , Christopher Cathcart , Steven O. Simmons , and Jonathan M. Horowitz 

^* Graduate Program in Genomic Sciences, Center for Comparative Medicine and Translational Research, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606; Graduate Program in Toxicology, Center for Comparative Medicine and Translational Research, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606; Department of Molecular Biomedical Sciences, Center for Comparative Medicine and Translational Research, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606; and Nikon Instruments, Melville, NY 11747

Submitted November 18, 2005; Revised January 25, 2006; Accepted February 2, 2006
Monitoring Editor: William Tansey

We have reported that extracts prepared from many human and mouse cell lines show little or no Sp2 DNA-binding activity and that Sp2 has little or no capacity to stimulate transcription of promoters that are activated by Sp1, Sp3, and Sp4. Using an array of chimeric Sp1/Sp2 proteins we showed further that Sp2 DNA-binding activity and trans-activation are each negatively regulated in mammalian cells. As part of an ongoing effort to study Sp2 function and regulation we characterized its subcellular localization in comparison with other Sp-family members in fixed and live cells. We report that 1) Sp2 localizes largely within subnuclear foci associated with the nuclear matrix, and 2) these foci are distinct from promyelocytic oncogenic domains and appear to be stable during an 18-h time course of observation. Deletion analyses identified a 37 amino acid sequence spanning the first zinc-"finger" that is sufficient to direct nuclear matrix association, and this region also encodes a bipartite nuclear localization sequence. A second nuclear matrix targeting sequence is encoded within the Sp2 trans-activation domain. We conclude that Sp2 preferentially associates with the nuclear matrix and speculate that this subcellular localization plays an important role in the regulation of Sp2 function.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Jonathan M. Horowitz (jon_horowitz{at}ncsu.edu).

This article has been cited by other articles:

				J. Xie, H. Yin, T. D. Nichols, J. A. Yoder, and J. M. Horowitz Sp2 Is a Maternally Inherited Transcription Factor Required for Embryonic Development J. Biol. Chem., February 5, 2010; 285(6): 4153 - 4164. [Abstract] [Full Text] [PDF]

				J. F.-X. Ainscough, F. A. Rahman, H. Sercombe, A. Sedo, B. Gerlach, and D. Coverley C-terminal domains deliver the DNA replication factor Ciz1 to the nuclear matrix J. Cell Sci., January 1, 2007; 120(1): 115 - 124. [Abstract] [Full Text] [PDF]