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Publications

Cardiovascular Biology Research Program

Laboratory of Membrane Structure & Function

William A. Rodgers, Ph.D. Assistant Member, Cardiovascular Biology Research Program Adjunct Assistant Professor, Departments of Microbiology & Immunology and   Pathology, University of Oklahoma Health Sciences Center

Research Interests
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.

Joined OMRF Scientific Staff in 1999.

Mailing Address
Cardiovascular Biology Research Program, MS 45
Oklahoma Medical Research Foundation
825 N.E. 13th Street
Oklahoma City, Oklahoma 73104

Contact Information
Phone: (405) 271-3550
Fax: (405) 271-7417
E-mail: William-Rodgers@omrf.org