The magician speaks the enchanted words, “Open Sesame!” and with the wave of a wand, a door opens.
Though it isn’t magic, cells are activated by signals that speak the “magic words,” activating pathways that lead to cell stimulation and growth. These signals communicate to cells through protein and lipid platforms that form in the membrane envelope of the cell.
In my lab, we study these membrane platforms in T cells, which are specialized cells that are important for the immune system. Our aim is to better understand the properties of the membrane platforms in order to affect immune responses. One area of interest is preventing atherosclerosis by altering the signals in the membrane platforms. Atherosclerosis begins as an inflammation in the wall of the artery that includes activated T cells. Learning how to inhibit the signals that activate T cells by altering the membrane platforms will be beneficial to preventing atherosclerosis and heart disease, which is a leading cause of death in the United States.
Since all cells are activated by signals in the membrane platforms, we collaborate with other scientists at OMRF to better understand diseases other than those caused by T cells. This includes Alzheimer’s disease and cancer. These collaborations in turn help us to better understand how the membrane platforms function in T cells.
Education
B.A., Westminster College, (magna cum laude), Fulton, Missouri, 1985
Ph.D., Biochemistry, University of Illinois/Urbana-Champaign, 1992
Honors and Awards
1985 The Cameron and Jesse Day Prize for Outstanding Biology Major, Westminster College
1986-1991 Eastman Kodak Predoctoral Fellowship
1991 Peer Recognition Award, Department of Biochemistry, University Illinois/Urbana-Champaign
1995-1996 National Research Service Award
1996 National Science Foundation Award for Young Biophysicists FASEB Summer Conference on Molecular Biophysics of Cellular Membranes
2005 The Merrick Award for Outstanding Research
Other Activities
Ad hoc reviewer: EMBO Journal, The Journal of Cell Science, The Journal of Immunology, The Journal of Virology, Trends in Immunology, The Scandinavian Journal of Immunology, National Science Foundation: National Institutes of Health
Institutional Service: Biohazards and Laboratory Safety Committee
Lecturer: Physical Biochemistry of Macromolecules (BIOC 6214), Department of Biochemistry and Molecular Biology 2nd year curriculum, University of Oklahoma Health Sciences Center
Student Advisory: Oklahoma Medical Research Foundation Fleming Scholars Summer Research Program; thesis advisor for Ph.D. graduate student, Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center; service on Ph.D. candidate thesis committees, Departments of Microbiology & Immunology and Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center
Memberships
American Association for the Advancement of Science
The American Society of Cell Biology
The American Association of Immunologists
Joined OMRF Scientific Staff in 1999.
Biological membranes are organized into discrete structural and functional domains. Establishing and maintaining this compartmentalization is important for the activation and regulation of membrane functions. For example, in the vascular system, enrichment of specific proteins in membrane domains in leukocytes, endothelial cells, and platelets is important towards leukocyte trafficking, hemostasis, and vasculature growth and remodeling. Similarly, membrane domains in lymphocytes compartmentalize cell signaling in response to antigen, including the specialized immunological synapse that forms in activated cells.
My laboratory studies the mechanisms by which membrane domains form, and their properties in activating and regulating associated membrane functions. Much of our work addresses the structure/function properties of the cholesterol-dependent membrane “raft” domains. Using fluorescence cell imaging, we recently identified an association between membrane rafts and the underlying cytoskeleton. We also showed these interactions are important in establishing rafts and in regulating raft-associated signaling molecules.
Our studies continue to identify novel functions for membrane rafts. Recently, using fluorescently labeled T cells, we showed that an actin-dependent clustering of membrane rafts is one of the earliest steps in T lymphocyte stimulation. Furthermore, enriched in the early raft clusters are raft-associated signaling proteins that are necessary for T cell activation, such as the T cell co-receptor CD4. Thus, the early clustering event establishes a membrane environment that is favorable for signaling from the T cell antigen receptor, and suggests a gatekeeper function in regulating the membrane environment at the site of T cell signaling.
We hypothesize that tuning raft-actin interactions to affect raft localization and membrane functions is a general principle of both vascular cells and cells of other organ systems. Long terms goals therefore include deciphering the mechanisms bringing about actin associations with membrane rafts, and how these interactions function in regulating signaling pathways localized in membrane rafts.
Recent Publications
Shao B, Yago T, Coghill PA, Klopocki AG, Mehta-D’Souza P, Schmidtke DW, Rodgers W, McEver RP. Signal-dependent slow leukocyte rolling does not require cytoskeletal anchorage of P-selectin glycoprotein ligand-1 (PSGL-1) or integrin alphaLbeta2. J Biol Chem 2012. [Abstract] EPub
Arbuckle JL, Rahman NS, Zhao S, Rodgers W, Rodgers KK. Elucidating the domain architecture and functions of non-core RAG1: the capacity of a non-core zinc-binding domain to function in nuclear import and nucleic acid binding. BMC Biochem 12:23, 2011. [Abstract]
Miner JJ, Shao B, Wang Y, Chichili GR, Liu Z, Klopocki AG, Yago T, McDaniel JM, Rodgers W, Xia L, McEver RP. Cytoplasmic domain of P-selectin glycoprotein ligand-1 facilitates dimerization and export from the endoplasmic reticulum. J Biol Chem 286:9577-9586, 2011. [Abstract]
Selected Publications
Chichili GR, Westmuckett A, Rodgers W. T cell signal regulation by the actin cytoskeleton. J Biol Chem 285:14737-14746, 2010. [Abstract]
Johnson CM, Rodgers W. Spatial segregation of phosphatidylinositol 4,5 biphosphate (PIP2) signaling in immune cell functions. Immunol Endocr Metabol Agents Med 8:349-357, 2008. [Abstract]
Chichili GR, Rodgers W. Clustering of membrane raft proteins by the actin cytoskeleton. J Biol Chem 282:36682-36691, 2007. [Abstract]
Van Komen JS, Mishra S, Byrum J, Chichili GR, Yaciuk JC, Farris AD, Rodgers W. Early and dynamic polarization of T cell membrane rafts and constituents prior to TCR stop signals. J Immunol. 179:6845-6855, 2007. [Abstract]
Rodgers W, Farris D, Mishra S. Merging complexes: properties of membrane raft assembly during lymphocyte signaling. Trends Immunol 26: 97-103, 2005. [Abstract]
Rodgers W, Rose JK. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. J Cell Biol 135:1515-1523, 1996. [Abstract]
Cardiovascular Biology Research Program, MS 45
Oklahoma Medical Research Foundation
825 N.E. 13th Street
Oklahoma City, OK 73104
Phone: (405) 271-3550
Fax: (405) 271-7417
E-mail: rodgersw@omrf.org
