R. Bryan Sutton, Ph.D.
Assistant Professor
- Affiliations:
Department of Neuroscience & Cell Biology
Sealy Center for Structural Biology and Molecular Biophysics - Route: 0620 4.212H Research Building 17
- Tel: (409) 772-1305
- Fax: (409) 747-2187
- rbsutton@utmb.edu
- Sutton Lab Webpage
- Dr. Sutton's Publications
- Dr. Sutton's CV
R. Bryan Sutton , Ph.D.
Education
• Bachelor of Science,
North Carolina State University, 1986
• Doctor of Philosophy,
The University of Texas Southwestern Medical Center, 1997
• Post-Doctoral Training,
Yale University (1997-2000) and Stanford University, 2000-2001
About the Lab
C2 domains are Ca+2-dependent/phospholipid binding proteins, which are crucial for manipulating biological membranes. My lab seeks to understanding the structure and function of C2 domain containing proteins using X-ray crystallography. Our primary interest is in human synaptotagmin 1. Consequently, we solved the X-ray structure of the complete cytosolic domain of synaptotagmin 1, and we are now investigating various mechanisms of action. We are also actively examining the C2 domains of human dysferlin that are linked to Limb-Girdle muscular dystrophy.
Through our collaboration with Introgen Therapeutics and M.D. Anderson Cancer Center in Houston, we are also investigating the 3D structure of interleukin-24. Human IL-24 is unique among the IL-10 superfamily as there is evidence that it possesses multiple anti-cancer properties, including direct tumor cell cytotoxicity, TH1 immune stimulation and anti-angiogenic activities. We are presently characterizing this promising cytokine using a variety of biochemical and biophysical techniques.
Selected Publications
Sutton, R.B., Davletov, B.A., Berghuis, A.M., Südhof, T.C., and Sprang, S.R.. Structure of the First C2 domain of Synaptotagmin I: A novel Ca+2/ phospholipid-binding Fold. Cell. 80:929–938; 1995.
Rizo, J., Sutton, R.B., Breslau, J., Koerber, S.C., Porter, J., Hagler, A.T., Gierasch, L., and Rivier, J. (1996). A Novel Conformation in a Highly Potent, Constrained Gonadotrophin Releasing Hormone Antagonist. Journal of the American Chemical Society, 118(5):970–976; 1996.
Shao, X. Davletov, B.A., Sutton, R.B., Sudhof, T.C. and Rizo, J. Bipartite Ca+2-binding Motif in C2 domains of Synaptotagmin and Protein Kinase C. Science. 273:248–251; 1996.
Fasshauer, D., Sutton, R.B., Brunger, A.T., and Jahn, R.. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R- SNAREs. Proceedings of the National Academy of Sciences USA, 95:15781-15786; 1998.
Sutton, R.B. and Sprang, S.R. Structure of the Protein Kinase Cb phospholipid-binding C2 domain complexed with Ca2+. Structure, 6(11):1395-1405; 1998.
Sutton, R.B., Fasshauer, D., Jahn, R., and Brunger, A.T. Crystal Structure of a SNARE Complex involved in synaptic exocytosis at 2.4 Å Resolution. Nature 395:347-353; 1998.
Sutton, R.B., Ernst, J., and Brunger, A.T. Crystal Structure of cytosolic C2A-C2B domains of synaptotagmin III. Journal of Cell Biology, 147:589-598; 1999.
Furst, H., Sutton, R.B., Brunger, A.T., Grigorieff, N., Three-Dimensional Structure of the AAA ATPase, NSF, at 11 Å resolution. EMBO J 22 (17):4365-4374; 2003.
Sieger, K.A., Mhashilkar, A.M., Stewart, A., Sutton, R.B., Strube, R.W., Chen, S-Y., Pataer, A., Swisher, S.G., Ramesh, R., Chada, S. The tumor suppressor activity of MDA-7/IL-24 is mediated by intracellular protein expression in NSCLC cells. Molecular Therapy 9(3), 355-367, 2004.
Chada,S., Mhashilkar, A.M., Ramesh, R., Mumm, J.B., Sutton R.B., Bocangel, D., Zheng, M., Grimm, E.A. and Ekmekcioglu, S., Bystander activity of Ad-mda7: Human MDA-7 protein kills melanoma cells via an IL-20 receptor-dependent but STAT3-independent mechanism, Molecular Therapy 10(6), 1085-1095, 2004.
Chada, S., Sutton, R.B., Ekmekcioglu, S., Ellerhorst, J., Mumm, J.B., Leitner, W.W., Yang, H.Y., Sahin, A.A., Hunt, K.K., Fuson, K.L., Poindexter, N., Roth, J.A., Ramesh, R., Grimm,E.A., Mhashilkar, A.M., MDA-7/IL-24 is a unique cytokine-tumor suppressor in the IL-10 family, Int Immunopharmacol. 4(5), 649-667, 2004.Sutton, R.B., Navarro, J.,Gurevich, V.V., X-ray crystal structure of Ambystoma cone arrestin at 2.3 Å resolution. Journal of Molecular Biology, 354(5), 1069-80, 2005. (in addition to cover art).
Peng, B-H., Anderson, J., Lee, J.C., Sutton, R.B.*, Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin. Acta Cryst., F61, 2005.
Montes, M, Fuson, KL., Sutton, RB*, and Robert, JJ. Purification, crystallization and X-ray diffraction analysis of human synaptotagmin 1 C2A-C2B.Acta Cryst. , F62, p.926, 2006.
Lagow, R.D., Bao, H., Cohen, E.N., Daniels, R.W., Zuzek, A., Williams, W.H., MacLeod, G.T., Sutton, R.B. and Zhang, B. Modification of a hydrophobic layer by a point mutation in Syntaxin 1A regulates the rate of synaptic vesicle fusion. PLoS Biology,5(4), e72, 2007.
Fuson, KL, Montes, M, Robert, JJ, Sutton, RB*. Structure of human synaptotagmin 1 C2AB in the absence of Ca+2 reveals a novel domain association. Biochemistry, 46, 13041-13048, 2007.(cover art).
Greene, D., T. Garcia, R. B. Sutton, K. M. Gernert, G. M. Benian, and A. F. Oberhauser. 2008. Single-molecule force spectroscopy reveals a stepwise unfolding of C. elegans giant protein kinase domains. Biophys Journal, 2008.