Office Phone: 318-675-5167
Laboratory Phone: 318-675-5173
Office Fax: 318-675-5180
Ph.D., 1976, University of Utah
Functions of GLUT1CBP (GIPC), a myosin VI adapter protein
We have identified an adapter protein, GLUT1CBP (now termed GIPC), which contains both a PDZ domain that binds to the C-terminal four amino acid residues of GLUT1 and a C-terminal domain that interacts with the tail domain of myosin VI. The movement of GIPC is microtubule-independent, actin-dependent, and occurs coordinately as a complex with myosin VI in a direction consistent with myosin VI-coupled movement. The large number of proteins identified by our laboratory and others that interact with the PDZ domain of GIPC implicate GIPC as an important adapter protein that links diverse cargos, bound by the PDZ domain, to cellular movement and targeting via the atypical motor protein myosin VI. This would suggest that one potential cellular function for GIPC is to provide an important protein/vesicle targeting and/or anchoring role for proteins that bind to its PDZ domain. Thus, our current efforts are focused upon examining the function of GIPC in regulating the distribution and movement of GLUT1 and other interacting proteins within the cell. Several of the newly identified interacting proteins participate in important pathways that regulate cell adhesion, cell division, motility, tight junction integrity, and the availability of sugar as an energy source for the cell. In particular, we have identified b-catenin as a new interacting partner, and have linked the b-catenin bound proteins E-cadherin in prostate cancer cells, and PECAM1 in endothelial cells to GIPC dependent redistribution. Therefore, our laboratory is interested in understanding the regulatory functions that GIPC might exert in these pathways that could alter diverse disease process, e.g., tumor progression in cancer and disrupted blood-brain-barrier function after stroke.
All Publications: PubMed