1988 — 1992
B.S. University of Dayton, Dayton, Ohio
1993 — 1998
Ph.D. University of Toledo, Toledo, Ohio
1999 — 2005
Postdoctoral Fellow, Cold Spring Harbor Laboratory, New York
Research in the Bubulya laboratory aims to understand the relationship between nuclear structure and gene expression. The nucleus of mammalian cells is divided into compartments that play vital roles in cellular processes such as DNA replication and repair, pre-messenger RNA synthesis and processing, and ribosome biogenesis. We would like to learn more about the mechanisms that regulate structural maintenance of nuclear domains. Our major focus is to understand the structural organization of nuclear speckles. Proteomic analysis of purified nuclear speckles showed that these domains contain pre-mRNA processing factors and many novel proteins that must be further characterized with regard to their nuclear functions (Saitoh, et al., 2004). We are currently examining the roles of Btf and Son in gene regulation. Son is a large insoluble nuclear protein with multiple unique repetitive domains. We hypothesize that Sonís unique repeats may be docking sites for recruitment, assembly and regulation of gene expression machinery in nuclear speckles or at gene loci (Takata et al., 2009; Sharma et al., 2010). Nuclear speckles show dynamic reorganization throughout mitosis, and studies are underway to decipher roles for nuclear speckle proteins in mitotic functions such as cell cycle progression or metaphase chromosome alignment. We would like to understand how daughter nuclei re-establish nuclear speckles to resume gene expression following mitosis.
Research Opportunities for Students
WSU undergraduate and graduate students seeking laboratory experience in cell and molecular biology should contact Dr. Paula Bubulya regarding project availability.
Sharma, A., M. Markey, K. Torres, S. Varia, M. Kadakia, A. Bubulya and P. A. Bubulya. 2011. Son Maintains Accurate Splicing for a Subset of Human Pre-mRNAs. J. Cell Sci. 124: 4286-4298. Highlighted “In this issue”: No Daughters without Son. J. Cell Sci. 124: e2403.
Tripathy, V., J. Ellis, Z. Shen, D. Song, S.M. Freier, F. C. Bennett, A. Sharma, P. A. Bubulya, B. Blencowe, S. G. Prasanth, K. V. Prasanth. Manuscript submitted.
- Chowdhury, A. G. Liu, M. Kemp, X. Chen, N. Katrangi, S. Meyers, M. Ghosh, J. Yao, Y. Gao, P. Bubulya and M. Leffak. 2010. The DNA unwinding element binding protein DUE-B interacts with Cdc45 in preinitiation complex formation. Mol. Cell Biol. 30:1495-1507.
- Sharma, A., H. Takata, K. Shibahara, A. Bubulya and P. A. Bubulya. 2010. Son is essential for nuclear speckle organization and cell cycle progression. Mol. Biol. Cell. 21:650-663.
- Takata, H. H. Nishijima, S. Ogura, T. Sakaguchi, P. A. Bubulya, T. Mochizuki and K. Shibahara. 2009. Proteome analysis of human nuclear insoluble fractions. Genes to Cells. 14:975-990.
- Su, M., K. Giang, K. Zumer, H. Jiang, I. Oven, J. L. Rinn, J. J. DeVoss, K. P. A. Johannes, W. Lu, J. Gardner, A. Chang, P. Bubulya, H. Y. Chang, B. M. Peterlin, and M. S. Anderson. 2008. Mechanisms of an autoimmunity syndrome in mice caused by a dominant mutation in Aire. J. Clin. Invest. 118:1712-1726.
- Bubulya P. A., K. V. Prasanth, T. J. Deerinck, D. Gerlich, J. Beaudouin, M. H. Ellisman, J. Ellenberg and D. L. Spector. 2004. Hypophosphorylated SR splicing factors transiently localize around active nucleolar organizing regions in telophase daughter nuclei. J. Cell Biol. 67:51-63.
- Saitoh, N., C. S. Spahr, S. Patterson, P. Bubulya, A. F. Neuwald and D. L. Spector. 2004. Proteomic analysis of interchromatin granule clusters. Mol. Biol. Cell. 15:3876-3890.
- Bubulya P. A. and D. L. Spector. 2004. “On the move”ments of nuclear components in living cells. Exp. Cell Res. 296:4-11.
- Prasanth K. V., P. A. Sacco-Bubulya, S. G. Prasanth and D. L. Spector. 2003. Sequential entry of components of the gene expression machinery into daughter nuclei. Mol. Biol. Cell. 14:1043-1057.
- Sacco-Bubulya P. A. and D. L. Spector. 2002. Disassembly of interchromatin granule clusters alters the coordination of transcription and pre-mRNA splicing. J. Cell Biol. 156:425-436.
- Wahl J.K., J. E. Nieset , P. A. Sacco-Bubulya, T. M. Sadler , K. R. Johnson and M. J. Wheelock. 2000. The amino- and carboxyl-terminal tails of beta-catenin reduce its affinity for desmoglein 2. J. Cell Sci.113: 1737-45.
- Solomon, D., P. A. Sacco, S. G. Roy, I. Simcha, K. R. Johnson, M. J. Wheelock and Avri Ben-Ze'ev. 1997. Regulation of beta-catenin levels and localization by overexpression of plakoglobin and inhibition of the ubiquitin-proteasome system. J. Cell Biol. 139:1325-1335.
- Wahl, J. K., P. A. Sacco, T. M. McGranahan-Sadler, L. M. Sauppe, M. J. Wheelock, and K. R. Johnson. 1996. Plakoglobin domains that define its association with the desmosomal cadherins and the classical cadherins: identification of unique and shared domains. J. Cell Sci. 109: 1143-1154.
- Sacco, P. A., T. M. McGranahan, M. J. Wheelock, and K. R. Johnson. 1995. Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin. J. Biol. Chem. 271: 20201-20205.