Steve Hartson

	Title	Director, Proteomics & Mass Spectrometry Core Facility
	Office	350A NRC
	Phone	405-744-6191
	Email	steven.hartson@okstate.edu
	Degree	Ph.D. Biochemistry. 1991. Oklahoma State University, Stillwater, OK
	Website	http://dnaproteincore.biochem.okstate.edu/

Research Area (top)

Dissecting the structure and function of an anti-cancer drug target

As one of the major cellular chaperones, Hsp90 plays diverse roles in supporting and regulating the proteins that control cell growth and division. Hsp90 function itself is regulated by a large diverse set of subunits. Previous work, in collaboration with Dr. Robert Matts, focused on the roles of Hsp90 in supporting kinase function. Dr. Hartson's team used gel-based "proteomics" techniques and mass spectrometry to discover new human Hsp90-binding proteins. Some of these new subunits have been described in yeast, while others are novel. Many of these new subunits are associated with the mitotic spindle, suggesting a role for Hsp90 in the tubulin-based cytoskeleton network. Future work will be directed at dissecting the function, structures, and mechanisms behind these new protein partnerships. Techniques will include molecular biology, cell culture and microscopy, and high-performance mass spectrometry.

Selected Publications (top)

Wang P, Chintagari NR, Narayanaperumal J, Ayalew S, Hartson S, Liu L. 2008.

Proteomic analysis of lamellar bodies isolated from rat lungs.  BMC Cell Biol. 9:34.

Arrese EL, Rivera L, Masakasu H, Mirza S, Hartson S, Weintraub S, and Soulages JL. 2008. Function and structure of lipid storage droplet protein 1 studied in lipoprotein complexes. Arch. Biochem. Biophys. 473, 42-47.

Te, J., Jia, L., Rogers, J., Miller, A., Hartson, S.D., (2007) Novel Subunits of the Mammalian Hsp90 Signal Transduction Chaperone,”J. Protome Research 6:1963-1973

Dabo S.M., Confer A.W., Hartson S.D. (2005) Adherence of Pasteurella multocida to fibronectin. Vet Microbiol. 110:265-75.

Prince, T., Shao, J., Matts, R.L. and Hartson, S.D. (2005) Evidence for Chaperone Heterocomplexes Containing Both Hsp90 and VCP. Biochem.Biophys. Res. Comm. 331(4), 1331-1337.

Ji, C., Wang, Y., Guo, X., Hartson, S.D. and Jiang, H. (2004) A Pattern Recognition Serine Proteinase Triggers the Prophenoloxidase Activation cascade in the Tobacco Hornworm, Naduca sexta. J. Biol. Chem. 279, 34101-34106.

Yun, B.G., Huang, W., Leach, N., Hartson, S.D. and Matts, R.L. (2004) Novobiocin Induces a Distinct Conformation of Hsp90 and Alters Hsp90-Cochaperone-Client Interactions. Biochemistry 43, 8217-8229.

Scroggins B.T., Prince, T., Shao, J., Uma, S., Huang, W., Guo, Y., Yun, B.G., Hedman, K., Matts, R.L., Hartson, S.D. (2003) High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients. Biochemistry 42:12550-61.

Shao, J., Prince, T., Hartson, S.D. and Matts, R.L. (2003) Phosphorylation of Serine 13 is required for the Proper Function of the Hsp90 Co-chaperone, Cdc37. J. Biol. Chem. 278(40), 38117-38120.

Shao, J., Irwin, A., Hartson, S.D. and Matts, R.L. (2003) Functional Dissection of Cdc37: Characterization of Domain Structure and Amino Acid Residues Critical for Protein Kinase Binding. Biochemistry 42, 12577-12588.

Scroggins, B.T., Shao, J., Prince, T., Uma, S., Huang, W., Guo, Y., Hedman, K., Matts, R.L. and Hartson, S. D. (2003) Conformational Switching of Hsp90 is triggered by Multiple Discrete Segments of Its Kinase Clients. Biochemistry 42, 12550-12561.

Shao, J., Hartson, S.D. and Matts, R.L. (2002) Evidence that Protein Phosphatase 5 Functions to Negatively Modulate the Maturation of the Hsp90-dependent Heme-regulated eIF2alpha Kinase. Biochemistry 41, 6770-6779.

Scholz, G.M., Hartson, S.D., Cartledge, K., Volk, L., Matts, R.L. and Dunn, A.R. (2001) The Molecular Chaperone Hsp90 is Required for Signal Transduction by Wild-Type Hck and Maintenance of Its Constitutively Active Counterpart. Cell Growth & Differentiation 12, 409-417.

Shao, J., Grammatikakis, N., Scroggins, B.T., Uma, S., Huang, W., Chen, J.-J., Hartson, S.D. and Matts, R.L. (2001) Hsp90 Regulates p50Cdc37 Function During the Biogenesis of the Active Conformation of the Heme-regulated eIF2 Kinase. J. Biol. Chem. 276, 206-214.

Yorgin, P.D., Hartson, S.D., Fellah, S.D., Scroggins, B.T., Huang, W., Matts, R.L. and Whitesell, L. (2000) Effects of Geldanamycin, an HSP90-binding Agent, on T-cell Function and T-cell Non-Receptor Protein Tyrosine Kinases. J. Immunology 164, 2915-2923.

Hartson, S.D., Irwin, A.D., Shao, J., Scroggins, B.T., Volk, L., Huang, W. and Matts, R.L. (2000) p50Cdc37 Is a Nonexclusive Hsp90 Cohort Which Participates Intimately in Hsp90-Mediated Folding of Immature Kinase Molecular. Biochemistry 39, 7631-7644.

Lab Members (top)