Paula Bubulya, Ph.D.

Associate Professor and Associate Chair
(937) 775-2403


  • 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/processing, and ribosome biogenesis. Proteomic analysis of purified nuclear speckles showed that nuclear speckles contain pre-mRNA processing factors, many of which remain to be characterized with regard to their specific nuclear functions.  Our ongoing research aims to determine the roles of three such proteins, Btf, TRAP150 and Son, in structural organization of nuclear speckles as well as in gene expression. Studies are also underway to examine functions for nuclear speckle proteins in progression of mitosis and maintenance of genome integrity.

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.


  1. Lu, Xinyi, J. Göke, F. Sachs, P.-É. Jacques, H. Liang, B. Feng, G. Bourque, P.A. Bubulya and H.-H. Ng. 2013. SON connects the splicing-regulatory network with pluripotency in human embryonic stem cells. Nat. Cell Biol. 15: 1141–1152.
  2. Varia, S., D. Potabathula, Z. Deng, A. Bubulya and P.A. Bubulya. 2013. Btf and TRAP150 have distinct roles in regulating subcellular mRNA distribution. Nucleus. 4:229-40.
  3. Leonard, M.K., N.T. Hill, P.A. Bubulya and M. Kadakia. The PTEN-Akt pathway impacts the integrity and composition of mitotic centrosomes. 2013. Cell Cycle. 12:1406-15.
  4. Bubulya A. and P. A. Bubulya. 2012. “Imaging cellular metabolism” in Paula A. Bubulya, ed., Cell Metabolism: Cell Homeostasis and Stress Response. Rijeka, Croatia: InTech.
  5. Sharma, A., M. Markey, K. Torres-Munoz, 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. 
  6. Peng, H.J., K. Henkels, M. Mhankali, C. Marchal, P. Bubulya, M. Dinauer and J. Cambronero.  2011. The small GTPase Rac2 inactivates PLD2 during chemotaxis by depriving the availability of phosphotidylinositol 4.5 bisphosphate. Mol. Cell Biol. 31:2227-40.
  7. Tripathi, 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.
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. Bubulya P. A. and D. L. Spector. 2004.  “On the move”ments of nuclear components in living cells.  Exp. Cell Res.  296:4-11.
  15. 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.
  16. 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.
  17. 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.
  18. 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.
  19. 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.
  20. 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.