Scott Emr is the Frank Rhodes Professor of Molecular Biology and Genetics and Director of the Weill Institute. Prior to joining Cornell, he held positions at Caltech and UCSD School of Medicine.
The Emr Lab studies the regulation of cell signaling and membrane trafficking pathways by phosphoinositide kinases, protein kinases, selective ubiquitin modifications, and vesicle-mediated transport reactions.
All eukaryotic cells maintain an elaborate system of vesicular transport pathways that convey cargo in and out of the cell via the endocytic and secretory systems. The Emr Lab's long-term goal has been to define the complex regulatory processes that ensure the temporal and spatial specificity of these membrane trafficking systems. Research has been focused in two major areas: (1) endocytic trafficking and receptor down-regulation and (2) phosphoinositide lipid- and ubiquitin-dependent membrane sorting pathways.
Research in the Emr Lab presently is focused in four major areas:
1. The assembly and function of each of the five complexes of the ESCRT pathway
2. Global screening to identifying novel genes/proteins necessary for trafficking transmembrane proteins through the endolysosomal membrane system
3. Regulation of endocytosis by arrestin-related ART proteins by selective ubiquitin modification of PM proteins
4. Regulation of synthesis and turnover of PIPs by lipid kinases and phosphatases
To learn more, please visit the Emr Lab website at: http://emr.wicmb.cornell.edu/
Awards and Honors
- van Deenan Medal "in recognition of his outstanding career in biomembrane research that includes discoveries of the role for polyphosphoinositol lipids (PIPs) in membrane trafficking, the role for the ESCRT machinery in receptor down-regulation, and for his identification of protein complexes (e.g., Retromer, HOPS, ART’s) that direct protein trafficking to the lysosome" (2014) University of Utrecht
- Tang, S., Henne, W. M., Borbat, P. P., Buchkovich, N. J., Freed, J., Mao, Y., Fromme, J. C., & Emr, S. D. (2015). Structural Basis for Activation, Assembly and Membrane Binding of ESCRT-III Snf7 Filaments. eLife. 2015(4).
- Li, M., Koshi, T., & Emr, S. D. (2015). Membrane-anchored ubiquitin ligase complex is required for the turnover of lysosomal membrane proteins. Journal of Cell Biology. 211:639-652.
- Henne, W. M., Zhu, L., Balogi, Z., Stefan, C., Pleiss, J. A., & Emr, S. D. (2015). Mdm1/Snx13 is a novel ER-endolysosomal interorganelle tethering protein. Journal of Cell Biology. 210:541-551.
- Henne, W. M., Liou, J., & Emr, S. D. (2015). Molecular mechanisms of inter-organelle ER-PM contact sites. Current Opinion in Cell Biology. 26:123-130.
- Li, M., Rong, Y., Chuang, Y., Peng, D., & Emr, S. D. (2015). Ubiquitin-dependent lysosomal membrane protein sorting and degradation. Molecular cell. 57:467–478.
- Buchkovich, N. J., Henne, W. M., Tang, S., & Emr, S. D. (2013). Essential N-Terminal Insertion Motif Anchors the ESCRT-III Filament during MVB Vesicle Formation. Developmental Cell. 27:201-214.
- Zhao, Y., Macgurn, J. A., Liu, M., & Emr, S. D. (2013). The ART-Rsp5 ubiquitin ligase network comprises a plasma membrane quality control system that protects yeast cells from proteotoxic stress. eLife. 2:e00459.
- Manford, A. G., Stefan, C., Yuan, H. L., MacGurn, J. A., & Emr, S. D. (2012). ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology. Developmental Cell. 23:1129-1140.
- Henne, W. M., Buchkovich, N. J., Zhao, Y., & Emr, S. D. (2012). The Endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices. Cell. 151:356-371.
- MacGurn, J. A., Hsu, P., & Emr, S. D. (2012). Ubiquitin and membrane protein turnover: from cradle to grave. Annual Review Biochemistry. 81:231-259.