Site Search



Lars Dreier, Ph.D.

Email Address:
larsdreier@ucla.edu

Laboratory Address:
Gonda Center, Room 3309


Mailing Address:
David Geffen School of Medicine at UCLA
Department of Neurobiology
695 Charles E. Young Dr. South
Gonda Center, Room 3309
Los Angeles, CA 90095

Office Address:
Gonda 3506C

UNITED STATES

Lab Number:
(310) 206-1701
Office Phone Number:
(310) 206-1701



Login to the Faculty Database

Department / Division Affiliations
Assistant Professor, Neuroscience IDP, Neurobiology
Member, ACCESS Program: Dept. of Neurobiology, Access Cell and Developmental Biology Home Area, Access Neuroscience Home Area, Brain Research Institute

Research Interest:

Molecular Mechanisms of Synapse Formation and Function in <i>C. elegans</i>

<p><font color="blue"> The formation of synapses between neurons and the regulation of signaling through these synapses is fundamental to the function of the nervous system. We are studying mechanisms of synapse formation and regulation of neurotransmitter receptors in the genetic model organism <i>C. elegans</i> using a combination of <b>genetic, cell biological, and biochemical techniques</b>.</p> <p>Analysis of the <i>C. elegans</i> nervous system is relatively easy due to the small number of neurons (302) and the fact that the connectivity between these neurons is known and identical in every animal. To visualize synapses, GFP- or RFP-tagged synaptic proteins can be expressed in subsets of neurons, for example the cholinergic or GABAergic motorneurons, or glutamatergic interneurons.</p> <p>Recent evidence indicates that regulated degradation of synaptic proteins is an important mechanism to control synapse formation and function. Ubiquitin-dependent degradation is a major pathway for regulated protein degradation. In this pathway, <b>ubiquitin ligases</b> conjugate the small protein ubiquitin to target proteins destined for degradation. We are currently characterizing the function of ubiquitin ligase mutants that affect synapse structure and synaptic transmission at various synapses. </p> <p>The activity of ubiquitin ligases is antagonized by <b>deubiquitinating enzymes</b> that remove ubiquitin from target proteins (in a similar way, protein kinases and phosphatases antagonize each other). Deubiquitinating enzymes are probably as important as ubiquitin ligases in regulating protein degradation, but very few have been characterized to date. The <i>C. elegans</i> genome encodes about 300 ubiquitin ligases and 50 deubiquitinating enzymes. In <b>RNAi based screens</b>, we are now identifying deubiquitinating enzymes that affect synaptic transmission and synapse structure. </font></p>

Bio:

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:

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 <i>C. elegans</i>. 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.