Ceresa, Brian P. (HSC)
The long-term goal of my laboratory is understand how signal transduction by cell surfacereceptors is regulated. Ultimately, we would like to develop strategies forselectively activating or inhibiting these cellular activities and bypass limitations of the receptor, such as low receptor number or receptor desensitization. Every extracellular ligand (growth factor, hormone, neurotransmitter, etc.)binds to a unique cell surface receptor that induces intracellular, biochemical changes that are integrated to invoke a specific change in cell physiology.While the exquisite specificity of this system has been long appreciated, the molecular mechanism by which it occurs is poorly understood. Understanding how an overlapping set of biochemical responses produces a specific physiology is the key to this problem. To address this question, we are using the prototypical receptor tyrosine kinase, the epidermal growth factor receptor(EGFR), as a model. The EGFR is critical for many developmental and homeostatic processes. In addition, overexpression of the EGFR is associated with many cancers.
Transforming Growth Factor-[alpha] (TGF-[alpha]) Enhances Corneal Epithelial Cell Migration by Promoting EGFR Recycling
McClintock, J.L. and Ceresa, B.P.
Rab7 Regulates Late Endocytic Trafficking Downstream of MVB Biogenesis and Cargo Sequestration
Vandlandingham, P.A. and Ceresa, B.P.
EGFR-mediated apoptosis of MDA-MB-468 cells requires receptor Internalization
Hyatt, D. and Ceresa, B.P.
Rab7 Activity Affects EGF:EGFR Degradation by Regulating Endocytic trafficking from the Late Endosome
Ceresa, B.P. and Bahr, S. J.
Continual expression of Rab5(Q79L) causes a ligand-independent EGFR internalization and diminishes EGFR activity
Dinneen, J. L. and Ceresa, B. P.