Dr. Vandenberg received her B.A. degree in Biology and Chemistry from the University of California, Santa Cruz, and her Ph.D. in Neurosciences from the University of California, San Diego. Her doctoral dissertation examined the biochemistry of visual transduction. As an NIH postdoctoral fellow and a Muscular Dystrophy Association postdoctoral fellow at UCLA, she studied sodium and potassium channels in nerve and muscle cells. Her research at UCSB uses molecular, cell biological and biophysical approaches to elucidate the mechanisms of ion channel function, protein trafficking and neuronal polarity.
Neurons and other excitable cells have the unique ability to transmit and to respond to signals on a millisecond time scale. These rapid signals are due to ion channels, which are the molecular gates that control electrical activity. Our research focuses on a) potassium channels and the signal transduction complexes that are involved in their regulation and trafficking, and b) mechanisms of neuronal polarity. Using a combination of cell biological and biophysical approaches, our goal is to learn how molecular events shape the electrical signals and responses of the nervous system.
Soo Hoo, L., Banna, C. D., Radeke, C. M., Sharma, N., Albertolle, M. E., Low, S. H., Weimbs, T., and Vandenberg, C. A. (2016) The SNARE protein syntaxin 3 confers specificity for polarized axonal trafficking in neurons. PLoS One 11(9), e0163671. doi:10.1371/journal.pone.0163671.
Wang, X., He, L., Vandenberg, C. A., and Montell, D. (2015) Imaging in optogenetics. In: Optical Probes in Biology; Zhang, J, Mehta, S., and Schultz, C., eds., CRC Press.
Dassau, L., Conti, L. R., Radeke, C. M., Ptáček, L. J., and Vandenberg, C. A. (2011) Kir2.6 regulates the surface expression of Kir2 inward rectifier potassium channels. J. Biol. Chem. 286, 9526-9541.
Adelman, J. P., Clapham, D. E., Hibino, H., Inanobe, A., Jan, L. Y., Karschin, A., Kubo, Y., Kurachi, Y., Lazdunski, M., Miki, T., Nichols, C. G., Pearson, W. L., Seino, S., and Vandenberg, C. A. (2008) Inwardly Rectifying Potassium Channels. IUPHAR/BPS Guide to Pharmacology, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=74
Fang, Y., Schram, G., Romanenko, V., Shi, C., Conti, L., Vandenberg, C. A., Davies, P. F., Nattel, S., and Levitan, I. (2005) Functional expression of Kir2.x in human aortic endothelial cells: the dominant role of Kir2.2. Am. J. Physiol. Cell Physiol. 289, C1134-1144.
Leonoudakis, D., Conti, L. R., Radeke, C. M., McGuire, L. M. M., and Vandenberg, C. A. (2004) A multi-protein trafficking complex composed of SAP97, CASK, Veli and Mint1 is associated with inward rectifier Kir2 potassium channels. J. Biol. Chem. 279, 19051-19063.
Leonoudakis, D., Conti, L. R., Anderson, S., Radeke, C. M., McGuire, L. M. M., Adams, M. E., Froehner, S. C., Yates, J. R., and Vandenberg, C. A. (2004) Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x) associated proteins J. Biol. Chem. 279, 22331-22346.
Conti, L.R., Radeke, C.M., and Vandenberg, C.A. (2002) Membrane targeting of ATP-sensitive potassium channel: Effects of glycosylation on surface expression. J. Biol. Chem. 277, 25416-25422.
Conti, L.R., Radeke, C.M., Shyng, S.-L., and Vandenberg, C.A. (2001) Transmembrane topology of the sulfonylurea receptor SUR1. J. Biol. Chem. 276, 41270-41278.