Mary Shannon Moore
Contact Information

Department of Medical Foundations
mmoore@rossu.edu

Mary Shannon Moore, PhD

Professor, Department of Medical Foundations

Mary Moore, PhD, was born and raised in Arlington, TX, and received her Bachelor of Science (BS) in Biology from Tulane University. In 1989, she received a Doctor of Philosophy (PhD) in Cell Biology from UT Southwestern Medical Center, Dallas, in the laboratory of Dr. Richard G.W. Anderson. Her dissertation research dealt with receptor-mediated endocytosis and the structure and function of clathrin-coated pits. From 1990 to 1994, she did a post-doctoral fellowship at Rockefeller University in New York, studying the mechanisms of nuclear protein import in the laboratory of Dr. Günter Blobel. 

In 1994, Dr. Moore joined the faculty of Baylor College of Medicine (BCM) in Houston in the Department of Molecular and Cellular Biology where she remained until she joined the Ross University School of Medicine faculty in 2004. At BCM, she continued her research on nuclear transport and, in 1996, was awarded a Searle Scholar award for this work. While at BCM, she lectured on Cell Biology to their first semester medical students, and was the co-director of the graduate course "Organization of the Cell.” In 1998, the BCM graduate students voted her best lecturer, and the class she and Dr. Pedersen co-directed won best overall graduate course in 2002 and 2004. At Ross, Dr. Moore lectures on Cell Biology and Histology in the first and second semesters and is the module director for the Fundamentals 1 module in semester 1. 

Areas of expertise
  • Cell Biology
  • Histology
Education and Certification
  • BS Tulane University
  • PhD in Cell Biology UT Southwestern
  • Post-doctoral fellowship Rockefeller University    
Honors and Awards
  • National Research Service Award Fellowship for Postdoctoral Study (1990-1993)
  • Searle Scholar 1996
  • Ron Taylor 2014
Affiliations and Memberships
  • ASCB (American Society for Cell Biology)
  • AAAS (American Association for the Advancement of Science)
Publications

1. Education

  • Sheakley M, Moore MS, Averill D, Grogan J, Davendranand S, Cystic Fibrosis Case for First Year Medical students - Team Based Learning Format. MedEdPORTAL; 2008. Available here
  • Sheakley M, Conran P, Moore M, LaVille A, Inflammation and Blood Clotting Case for First Year Medical Students - Team Based Learning Format. MedEdPORTAL; 2009. Available here
  • Sheakley M, Larsen N, Moore M, Wright B, Neurological Disorder Case for First Year Medical Students - Team Based Learning (TBL) Format . MedEdPORTAL; 2010. Available here
  • Gill D, Moore M, Winston K, Larsen N, Yin A, Callender D, Thomas V. A Thyroid Case for Year-One Medical Students. MedEdPORTAL; 2014. Available here

 

2. Clinical

  • Arrington, A.S., Moore, M.S., and Butel, J.S. (2004). SV40-positive brain tumor in scientist with laboratory exposure to virus. Oncogene 23, 2231-2235

 

3. Basic Science

  • Moore, M.S., Mahaffey, D.T., Brodsky, F.M., and Anderson, R.G.W. (1987). Assembly of clathrin-coated pits onto purified plasma membranes. Science 236, 558-563
  • Mahaffey, D.T., Moore, M.S., Brodsky, F.M., and Anderson, R.G.W. (1989). Coat proteins isolated from clathrin-coated vesicles can assemble into coated pits. J. Cell Biol. 108, 1615-1624
  • Moore, M.S., and Anderson, R.G.W. (1989). Towards an in vitro system for studying clathrin-coated pit function. J. Cell Sci. Suppl. 11, 179-186
  • Lin, H.C., Moore, M.S., Sanan, D.A., and Anderson, R.G.W. (1991). Reconstitution of clathrin-coated pit budding from plasma membranes. J. Cell Biol. 114, 881-891
  • Moore, M.S., and Blobel, G. (1992). The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors. Cell 69, 939-950
  • Moore, M.S., and Blobel G. (1993). The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature 365, 661-663
  • Moore, M.S., and Blobel, G. (1994). Purification of a Ran-interacting protein that is required for protein import into the nucleus. Proc. Natl. Acad. Sci. USA 91, 10212-10216
  • Radu, A., Blobel, G., and Moore, M.S. (1995). Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc. Natl. Acad. Sci. USA 92, 1769-1773
  • Ren, M., Villamarin, A., Shih, A., Coutavas, E., Moore, M.S., LoCurcio, M., Clarke, V., Oppenheim, J., D'Eustachio, P., and Rush, M.G. (1995). Separate domains of the Ran GTPase interact with different downstream effectors to regulate nuclear protein import and RNA processing. Mol. Cell. Biol. 15, 2117-2124
  • Radu, A., Moore, M.S., and Blobel, G. (1995). The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex. Cell 81, 215-222
  • Moore, M.S. and Blobel, G (1995). Soluble factors required for nuclear protein import. Cold Spring Harbor Sym. on Quant. Biol. Vol. LX, 701-705. 
  • Murphy, G., Moore, M.S., Drivas, G., Pérez de la Ossa, P., Villamarin, A., D’Eustachio, P., and Rush, M.G. (1997). A T42A Ran mutation: differential interactions with effectors and regulators, and defect in nuclear protein import. Mol. Biol. Cell 8, 2591-2604.
  • Popov, S., Rexach, M., Zybarth, G., Reiling, N., Lee, M.A., Ratner, L., Lane, C.M., Moore, M.S., Blobel, G., and Bukrinsky, M. (1998). Viral protein R (VPR) regulates nuclear import of the HIV-1 preintegration complex. EMBO J. 17, 101-109.
  • Feldherr, C., Akin, D., and Moore, M.S. (1998). The nuclear import factor p10 regulates the functional size of the nuclear pore complex during oogenesis. J. Cell Sci. 111, 1889-1896.
  • Schwoebel, E.D., Talcott, B., Cushman, I., and Moore, M.S. (1998). Ran dependent signal-mediated nuclear import does not require GTP hydrolysis by Ran.  J. Biol. Chem. 273, 35170-35175.
  • Kent, H.M., Moore, M.S., Quinby, B.B., Baker, A.M.E., McCoy, A.J. , Murphy, G. A., Corbett, A. H., and M. Stewart (1999).  Engineered Mutants in the Switch II Loop of Ran Define the Contribution made by Key Residues to the Interaction with Nuclear Transport Factor 2 (NTF2) and the Role of this Interaction in Nuclear Protein Import. J. Mol. Biol. 289, 565-77
  • Talcott, B. and Moore, M.S. (2000). The nuclear import of RCC1 requires a specific nuclear localization sequence receptor, karyopherin a3/Quip. J. Biol. Chem. 275, 10099-10104.
  • Lane, C.M., Cushman, I. and Moore, M.S. (2000). Selective disruption of nuclear import by a functional mutant nuclear transport carrier. J. Cell Biol. 151, 321-332. (Commentary in Science 290: 901, 2000).
  • Wiese, C., Merdes, A, Wilde, A., Moore, M.S., Adam, S.A., and Zheng, X. (2001). Importin-b couples Ran to downstream targets in microtubule assembly. Science 291, 653-656.
  • Whitehurst, A.W., Wilsbacher, J.L., Youngjai, Y., Luby-Phelps, K., Moore, M.S., and Cobb, M.S. (2002). ERK2 enters the nucleus by a carrier-independent mechanism. Proc. Natl. Acad. Sci. USA  99, 7496-7501.
  • Schwoebel, E.D., Ho, T., and Moore, M.S. (2002). The mechanism of inhibition of Ran-mediated nuclear transport by cellular ATP depletion. J. Cell Biol. 157, 963-974.
  • Chang, D.F., Belaguli, N.S, Iyer, D., Roberts, W.B., Marx, J.G., Wu, S., Dong, X.R., Marx,
  • J.G., Moore, M.S., Beckerle, M.C., Majesky, M.W., and Schwartz, R.J. (2003). Cysteine-rich LIM-only proteins, CRP1 and CRP2, are potent smooth muscle differentiation cofactors. Developmental Cell 4, 107-118.
  • Cushman, I., Stenoien, D, and Moore, M.S. (2004). The dynamic association of RCC1 with chromatin is modulated by Ran-dependent nuclear transport. Mol. Biol. Cell 5, 45-55.
  • Whitehurst, A.W., Robinson, F., Moore, M.S., and Cobb, M.H. (2004). The death effector domain protein PEA-15 inhibits nuclear entry of ERK2 by inhibiting required interactions. J. Biol. Chem. 279, 12840-12847.
  • Cushman, I., Bowman, B.R., Sowa, M.E., Lichtarge, O., Quiocho, F.A., and Moore, M.S. (2004).  Computational and biochemical identification of a nuclear pore complex binding site on the nuclear transport carrier NTF2. J. Mol. Biol. 344, 303-10.
  • Umeda. M., Isaddoost, S., Cushman, I., Moore, M.S., and Sazer, S. (2005). The fission yeast Schizosaccharomyces pombe has two importin alpha homologs, Imp1p and Cut15p, which have common and unique functions in nucleocytoplasmic transport and cell cycle progression. Genetics 171, 7-21.
  • Cushman, I., Palzkill, T., and Moore, M.S. (2006). Using peptide arrays to define nuclear carrier binding sites on nucleoporins. Methods 39, 329-41.
  • Moore, M.S., and Blobel, G. (1994).  A G-protein involved in nucleocytoplasmic transport: the role of Ran. Trends Biochem. Sci. 19, 211-216.
  • Moore, M.S. (1995). David and Goliath in nuclear transport. Current Biology 5, 1339-1341.
  • Moore, M.S. (1996). Nuclear export - out of the dark. Current Biology 6, 137-141.
  • Moore, M.S. (1996). Generation of GTP-Ran for nuclear protein import. Science 272, 47.
  • Moore, M.S. (1998). Ran and nuclear transport. J. Biol. Chem. 273, 22857-22860.
  • Talcott, B. and Moore, M.S. (1999). Getting across the nuclear pore complex. Trends Cell Biol. 9, 312-318.
  • Moore, M.S. (2003). Npap60: a new player in nuclear protein import. Trends Cell Biol. 13, 61-64.
  • Schwoebel, E.D. and Moore, M.S. (2000). “The control of gene expression by regulated nuclear transport”. Essays in Biochemistry-Molecular Trafficking. P. Bernstein ed. Portland Press, London. pp 105-113.
  • Moore, M.S. and E.D.Schwoebel (2000). "Nuclear transport assays using permeabilized cells".  Current Protocols in Cell Biology (supplement 5). J.S. Bonifacino, M.Dasso, H.B. Harford, J. Lippincott-Schwartz and K.H. Yamada eds. John Wiley and Sons, New York. pp.11.7.1-13.
  • Moore, M.S. (2001). "The role of Ran in nuclear import", The Small GTPase Ran, M. Rush and P. D'Eustachio, eds., Kluwer Academic Publishers, Norwell, MA. pp 1-11.
  • Moore, M.S. (2002). "Ran GTPase". The Encyclopedia of Molecular Medicine, T.M. Creighton,ed. John Wiley and Sons, New York. pp. 2726-2728.
  • Moore, M.S. (2004) "Ran GTPase". Encyclopedia of Biological Chemistry (W.J. Lennarz & M.D. Lane, eds), Elsevier, Oxford, Vol.3, pp. 635 - 639.