Biography
Dr. Lars Dreier joined the Department of Neurobiology as an Assistant Professor in 2006. Lars did his Ph.D. work in the Department of Cell Biology, Harvard Medical School, Boston, in the lab of Tom Rapoport, reconstituting the transport of secretory proteins through the Endoplasmic Reticulum (ER) membrane and characterizing the formation of the ER in vitro. In 2000, he joined the lab of Josh Kaplan at the University of California, Berkeley, where he started to work on ubiquitin-dependent regulation of glutamate receptors in C. elegans . Lars moved with the Kaplan lab back to Boston in 2002.
Publications
A selected list of publications:
Sun Yu, Vashisht Ajay A, Tchieu Jason, Wohlschlegel James A, Dreier Lars Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy The Journal of biological chemistry, 2012; 287(48): 40652-60.
Wang, J, G.W. Farr, D.H. Hall, F. Li, K. Furtak, L. Dreier, A.L. Horwich An ALS-Linked Mutant SOD1 Produces a Locomotor Defect Associated with Aggregation and Synaptic Dysfunction When Expressed in Neurons of Caenorhabditis elegans PLoS Genetics, 2009; 5(1): .
Dreier, L.* Burbea, M.* Kaplan, J. M. LIN-23-mediated degradation of beta-catenin regulates the abundance of GLR-1 glutamate receptors in the ventral nerve cord of C. elegans Neuron, 2005; 46: 51-64.
Burbea, M.* Dreier, L.* Dittman, J. S. Grunwald, M. E. Kaplan, J. M. Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans Neuron, 2002; 35: 107-20, * contributed equally.
Felbor, U. Dreier, L. Bryant, R. A. Ploegh, H. L. Olsen, B. R. Mothes, W. Secreted cathepsin L generates endostatin from collagen XVIII Embo J, 2000; 19(6): 1187-94.
Dreier, L. Rapoport, T. A. In vitro formation of the endoplasmic reticulum occurs independently of microtubules by a controlled fusion reaction J Cell Biol, 2000; 148(5): 883-98.
Panzner, S. Dreier, L. Hartmann, E. Kostka, S. Rapoport, T. A. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p Cell, 1995; 81(4): 561-70.