Paula Bubulya, Ph.D.

Associate Professor and Associate Chair
Biology
(937) 775-2403
paula.bubulya@wright.edu

Education

  • 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: 

Pre-mRNA processing is an essential feature of gene expression in eukaryotic cells. Coordination of gene expression and cell cycle progression is critical for cellular health. Nuclear speckles contain pre-mRNA processing factors, many of which remain to be characterized with regard to their specific nuclear functions and human disease relevance. Nearly 200 mRNA processing proteins have been identified, yet little is known about how these factors assemble into functional complexes within human cell nuclei. Our lab recently discovered that two related mRNA processing proteins, Btf and TRAP150, have critical roles in cell cycle regulation. Ongoing research in the Bubulya laboratory aims to define mechanistic functions for Btf, TRAP150 and SON in fundamental cellular processes including nuclear speckle organization, gene regulation, and cell cycle control. 

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.

Publications

Publications: (graduate students underlined)

  1. Battini, V.P., A. Bubulya and P.A. Bubulya. 2015. Accurate splicing of HDAC6 Pre-mRNA requires SON. Int. J. Mol. Sci. 16:5886-5899. doi:10.3390/ijms16035886.
  2. Lu, X., H.-H. Ng and P.A. Bubulya. 2014. The role of SON in splicing, development and disease. Wiley Interdisciplinary Reviews (WIREs) RNA. doi: 10.1002/wrna.1235  PMCID: PMC4138235
  3. 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. . PMID: 24013217; PMCID: PMC4097007; Comment in EMBO J. “Let’s Sp(l)ice up pluripotency!” Nov 13;32(22):2903-4.
  4. 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. PMID: 23778535; PMCID: PMC3720753
  5. 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. PMID: 23574721; PMCID: PMC3674068
  6. 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. Open Access. ISBN 978-953-307-978-3
  7. 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.  PMID: 22193954; PMCID: PMC3258111
  8. Peng, H.J., K. Henkels, M. Mhankali, C. Marchal, P. Bubulya, M. Dinauer and J. Cambronero.  2011. The Dual Effect of Rac2 on Phospholipase D2 Regulation That Explains both the Onset and Termination of Chemotaxis. Mol. Cell Biol. 31:2227-40. PMID: 21444720; PMCID: PMC3133238  
  9. 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. Mol. Cell. 39:925-938. PMID: 20797886
  10. 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.
  11. 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. PMID: 20053686; PMCID: PMC2820428
  12. 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. PMID: 19695025
  13. 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. PMID: 18414681; PMCID: PMC2293336
  14. 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. PMID: 15479736; PMCID: PMC2172523
  15. 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.  PMID: 15169873; PMCID: PMC491843
  16. Bubulya P. A. and D. L. Spector. 2004.  “On the move”ments of nuclear components in living cells.  Exp. Cell Res.  296:4-11.
  17. 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. PMID: 12631722; PMCID: PMC151578
  18. 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. PMID: 11827980; PMCID: PMC2173333
  19. 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. PMID: 10769205
  20. 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.  PMID: 9382877; PMCID: PMC2140206
  21. 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. PMID: 8743961
  22. 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.  PMID: 7650039