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
- Keith R. Porter Award “in recognition of outstanding contributions to cell biology” (2017) American Society for Cell Biology
- Elected Foreign Member (2008) European Molecular Biology Organization
- Avanti Award for "key contributions in lipid signaling research" (2007) American Society for Biochemistry and Molecular Biology, Washington D.C.
- Elected Member (2007) National Academy of Sciences
- Elected Member (2004) American Academy of Arts and Sciences
- Sardana, R., Zhu, L., & Emr, S. D. (2018). Rsp5 Ubiquitin ligase–mediated quality control system clears membrane proteins mistargeted to the vacuole membrane. JCB: The Journal of Cell Biology. 217.
- Suzuki, S. W., & Emr, S. D. (2018). Membrane protein recycling from the vacuole/lysosome membrane. JCB: The Journal of Cell Biology. 217:1623-1632.
- Zhu, L., Jorgensen, J. R., Li, M., Chuang, Y. S., & Emr, S. D. (2017). ESCRTS function directly on the lysosome membrane to downregulate ubiquitinated lysosomal membrane proteins. eLIFE. 6:e26403.
- Guiney, E., Klecker, T., & Emr, S. D. (2016). Identification of the endocytic sorting signal recognized by the Art1-Rsp5 ubiquitin ligase complex. Molecular Biology of the Cell. 27:4043-54.
- Tang, S., Buchkovich, N. J., Henne, W. M., Sudeep, B., Yunjun, K., & Emr, S. D. (2016). ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro1 during MVB biogenesis. eLIFE. 2016.
- 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. JCB: The 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. JCB: The Journal of Cell Biology. 210:541-551.
- 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.
- 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.